LOCUS       NP_004361               3063 aa            linear   PRI 11-FEB-2025
DEFINITION  collagen alpha-1(XII) chain long isoform precursor [Homo sapiens].
ACCESSION   NP_004361
VERSION     NP_004361.3
DBSOURCE    REFSEQ: accession NM_004370.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 3063)
  AUTHORS   Naghipoor,K., Khosravi,T. and Oladnabi,M.
  TITLE     Whole exome sequencing identifies a novel variant in the COL12A1
            gene in a family with Ullrich congenital muscular dystrophy 2
  JOURNAL   Mol Biol Rep 50 (9), 7427-7435 (2023)
   PUBMED   37458870
  REMARK    GeneRIF: Whole exome sequencing identifies a novel variant in the
            COL12A1 gene in a family with Ullrich congenital muscular dystrophy
            2.
REFERENCE   2  (residues 1 to 3063)
  AUTHORS   Yao,W., Yao,Y., He,W., Zhao,C., Liu,D., Wang,G. and Wang,Z.
  TITLE     PABPC1 promotes cell proliferation and metastasis in pancreatic
            adenocarcinoma by regulating COL12A1 expression
  JOURNAL   Immun Inflamm Dis 11 (7), e919 (2023)
   PUBMED   37506150
  REMARK    GeneRIF: PABPC1 promotes cell proliferation and metastasis in
            pancreatic adenocarcinoma by regulating COL12A1 expression.
REFERENCE   3  (residues 1 to 3063)
  AUTHORS   Tang,Z., Yang,Y., Zhang,Q. and Liang,T.
  TITLE     Epigenetic dysregulation-mediated COL12A1 upregulation predicts
            worse outcome in intrahepatic cholangiocarcinoma patients
  JOURNAL   Clin Epigenetics 15 (1), 13 (2023)
   PUBMED   36694230
  REMARK    GeneRIF: Epigenetic dysregulation-mediated COL12A1 upregulation
            predicts worse outcome in intrahepatic cholangiocarcinoma patients.
            Erratum:[Clin Epigenetics. 2023 Mar 21;15(1):46. doi:
            10.1186/s13148-023-01455-3.. PMID: 36945022]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 3063)
  AUTHORS   Papanicolaou,M., Parker,A.L., Yam,M., Filipe,E.C., Wu,S.Z.,
            Chitty,J.L., Wyllie,K., Tran,E., Mok,E., Nadalini,A., Skhinas,J.N.,
            Lucas,M.C., Herrmann,D., Nobis,M., Pereira,B.A., Law,A.M.K.,
            Castillo,L., Murphy,K.J., Zaratzian,A., Hastings,J.F.,
            Croucher,D.R., Lim,E., Oliver,B.G., Mora,F.V., Parker,B.L.,
            Gallego-Ortega,D., Swarbrick,A., O'Toole,S., Timpson,P. and
            Cox,T.R.
  TITLE     Temporal profiling of the breast tumour microenvironment reveals
            collagen XII as a driver of metastasis
  JOURNAL   Nat Commun 13 (1), 4587 (2022)
   PUBMED   35933466
  REMARK    GeneRIF: Temporal profiling of the breast tumour microenvironment
            reveals collagen XII as a driver of metastasis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 3063)
  AUTHORS   Li,Y., Su,Z., Wei,B., Qin,M. and Liang,Z.
  TITLE     Bioinformatics analysis identified MMP14 and COL12A1 as
            immune-related biomarkers associated with pancreatic adenocarcinoma
            prognosis
  JOURNAL   Math Biosci Eng 18 (5), 5921-5942 (2021)
   PUBMED   34517516
  REMARK    GeneRIF: Bioinformatics analysis identified MMP14 and COL12A1 as
            immune-related biomarkers associated with pancreatic adenocarcinoma
            prognosis.
REFERENCE   6  (residues 1 to 3063)
  AUTHORS   Berthod,F., Germain,L., Guignard,R., Lethias,C., Garrone,R.,
            Damour,O., van der Rest,M. and Auger,F.A.
  TITLE     Differential expression of collagens XII and XIV in human skin and
            in reconstructed skin
  JOURNAL   J Invest Dermatol 108 (5), 737-742 (1997)
   PUBMED   9129225
REFERENCE   7  (residues 1 to 3063)
  AUTHORS   Gerecke,D.R., Olson,P.F., Koch,M., Knoll,J.H., Taylor,R.,
            Hudson,D.L., Champliaud,M.F., Olsen,B.R. and Burgeson,R.E.
  TITLE     Complete primary structure of two splice variants of collagen XII,
            and assignment of alpha 1(XII) collagen (COL12A1), alpha 1(IX)
            collagen (COL9A1), and alpha 1(XIX) collagen (COL19A1) to human
            chromosome 6q12-q13
  JOURNAL   Genomics 41 (2), 236-242 (1997)
   PUBMED   9143499
REFERENCE   8  (residues 1 to 3063)
  AUTHORS   Walchli,C., Koch,M., Chiquet,M., Odermatt,B.F. and Trueb,B.
  TITLE     Tissue-specific expression of the fibril-associated collagens XII
            and XIV
  JOURNAL   J Cell Sci 107 (Pt 2), 669-681 (1994)
   PUBMED   8207089
REFERENCE   9  (residues 1 to 3063)
  AUTHORS   Oh,S.P., Taylor,R.W., Gerecke,D.R., Rochelle,J.M., Seldin,M.F. and
            Olsen,B.R.
  TITLE     The mouse alpha 1(XII) and human alpha 1(XII)-like collagen genes
            are localized on mouse chromosome 9 and human chromosome 6
  JOURNAL   Genomics 14 (2), 225-231 (1992)
   PUBMED   1427837
REFERENCE   10 (residues 1 to 3063)
  AUTHORS   Sugrue,S.P., Gordon,M.K., Seyer,J., Dublet,B., van der Rest,M. and
            Olsen,B.R.
  TITLE     Immunoidentification of type XII collagen in embryonic tissues
  JOURNAL   J Cell Biol 109 (2), 939-945 (1989)
   PUBMED   2668306
  REMARK    Erratum:[J Cell Biol 1989 Nov;109(5):following 2254]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL080250.11, DA661773.1,
            BP286308.1, AL354664.12, U73778.1, AL096771.11 and AI752603.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 21, 2006 this sequence version replaced NP_004361.2.
            
            Summary: This gene encodes the alpha chain of type XII collagen, a
            member of the FACIT (fibril-associated collagens with interrupted
            triple helices) collagen family. Type XII collagen is a homotrimer
            found in association with type I collagen, an association that is
            thought to modify the interactions between collagen I fibrils and
            the surrounding matrix. Alternatively spliced transcript variants
            encoding different isoforms have been identified. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (long) represents a transcript
            that encodes an isoform longer than that of the short isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U73778.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000322507.13/ ENSP00000325146.8
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..3063
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13-q14.1"
     Protein         1..3063
                     /product="collagen alpha-1(XII) chain long isoform
                     precursor"
                     /note="collagen type XII proteoglycan; collagen
                     alpha-1(XII) chain; collagen, type XII, alpha 1"
                     /calculated_mol_wt=330845
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2322
     mat_peptide     24..3063
                     /product="collagen alpha-1(XII) chain long isoform"
                     /calculated_mol_wt=330845
     Region          26..105
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            order(102..103,105..106)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          139..302
                     /region_name="vWA_collagen_alphaI-XII-like"
                     /note="Collagen: The extracellular matrix represents a
                     complex alloy of variable members of diverse protein
                     families defining structural integrity and various
                     physiological functions. The most abundant family is the
                     collagens with more than 20 different...; cd01482"
                     /db_xref="CDD:238759"
     Site            order(146,148,150,217,250)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238759"
     Site            order(148..150,152,217)
                     /site_type="active"
                     /note="integrin-collagen binding site [active]"
                     /db_xref="CDD:238759"
     Site            329
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:32337544; propagated from
                     UniProtKB/Swiss-Prot (Q99715.2)"
     Region          336..415
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            order(412..413,415..416)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          439..602
                     /region_name="vWA_collagen_alphaI-XII-like"
                     /note="Collagen: The extracellular matrix represents a
                     complex alloy of variable members of diverse protein
                     families defining structural integrity and various
                     physiological functions. The most abundant family is the
                     collagens with more than 20 different...; cd01482"
                     /db_xref="CDD:238759"
     Site            order(446,448,450,517,550)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238759"
     Site            order(448..450,452,517)
                     /site_type="active"
                     /note="integrin-collagen binding site [active]"
                     /db_xref="CDD:238759"
     Region          634..719
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            700
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99715.2)"
     Site            order(709..710,712..713)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          724..805
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            798
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99715.2)"
     Region          799..830
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99715.2)"
     Site            order(800..801,803..804)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          817..892
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Region          862..864
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99715.2)"
     Site            889
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99715.2)"
     Region          906..986
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            981
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99715.2)"
     Site            order(983..984,986..987)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          1002..1075
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Region          1077..1099
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99715.2)"
     Region          1090..1176
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(1165..1166,1168..1169)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          1198..1361
                     /region_name="vWA_collagen_alphaI-XII-like"
                     /note="Collagen: The extracellular matrix represents a
                     complex alloy of variable members of diverse protein
                     families defining structural integrity and various
                     physiological functions. The most abundant family is the
                     collagens with more than 20 different...; cd01482"
                     /db_xref="CDD:238759"
     Site            order(1205,1207,1209,1276,1309)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238759"
     Site            order(1207..1209,1211,1276)
                     /site_type="active"
                     /note="integrin-collagen binding site [active]"
                     /db_xref="CDD:238759"
     Region          1387..1465
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Region          1419..1986
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            order(1462..1463,1465..1466)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          1756..1834
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            1763
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99715.2)"
     Region          2028..2105
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Region          2118..2197
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(2192..2193,2195..2196)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            2206
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99715.2)"
     Region          2207..2282
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            order(2280..2281,2283..2284)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          2283..2312
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99715.2)"
     Region          2322..2486
                     /region_name="vWA_collagen_alphaI-XII-like"
                     /note="Collagen: The extracellular matrix represents a
                     complex alloy of variable members of diverse protein
                     families defining structural integrity and various
                     physiological functions. The most abundant family is the
                     collagens with more than 20 different...; cd01482"
                     /db_xref="CDD:238759"
     Site            order(2329,2331,2333,2401,2434)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238759"
     Site            order(2331..2333,2335,2401)
                     /site_type="active"
                     /note="integrin-collagen binding site [active]"
                     /db_xref="CDD:238759"
     Region          2451..2746
                     /region_name="Nonhelical region (NC3)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99715.2)"
     Region          2520..2712
                     /region_name="TSPN"
                     /note="Thrombospondin N-terminal -like domains;
                     smart00210"
                     /db_xref="CDD:214560"
     Site            2528
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q99715.2)"
     Site            2679
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q99715.2)"
     Region          2743..2896
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99715.2)"
     Region          2747..2898
                     /region_name="Triple-helical region (COL2) with 1
                     imperfection"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99715.2)"
     Region          <2764..>2897
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          2779..2781
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99715.2)"
     Region          2895..2897
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99715.2)"
     Region          2899..2941
                     /region_name="Nonhelical region (NC2)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99715.2)"
     Region          2932..3063
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99715.2)"
     Region          2942..3044
                     /region_name="Triple-helical region (COL1) with 2
                     imperfections"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99715.2)"
     Site            2944
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q99715.2)"
     Site            2947
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q99715.2)"
     Site            2950
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q99715.2)"
     Site            2959
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q99715.2)"
     Site            2965
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q99715.2)"
     Site            2968
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q99715.2)"
     Site            2971
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q99715.2)"
     Site            2983
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q99715.2)"
     Site            3000
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q99715.2)"
     Site            3003
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q99715.2)"
     Site            3014
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q99715.2)"
     Site            3023
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q99715.2)"
     Site            3026
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q99715.2)"
     Site            3029
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q99715.2)"
     Region          3045..3063
                     /region_name="Nonhelical region (NC1)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99715.2)"
     CDS             1..3063
                     /gene="COL12A1"
                     /gene_synonym="BA209D8.1; BTHLM2; COL12A1L; DJ234P15.1;
                     EDSMYP; UCMD2"
                     /coded_by="NM_004370.6:313..9504"
                     /note="long isoform precursor is encoded by transcript
                     variant long"
                     /db_xref="CCDS:CCDS43482.1"
                     /db_xref="GeneID:1303"
                     /db_xref="HGNC:HGNC:2188"
                     /db_xref="MIM:120320"
ORIGIN      
        1 mrsrlppala algaalllss ieaevdppsd lnfkiident vhmswakpvd pivgyritvd
       61 pttdgptkef tlsasttetl lselvpetey vvtitsydev eesvpvigql tiqtgsstkp
      121 vekkpgktei qkcsvsawtd lvflvdgsws vgrnnfkyil dfiaalvsaf digeektrvg
      181 vvqyssdtrt efnlnqyyqr dellaaikki pykggntmtg daidylvknt ftesagarvg
      241 fpkvaiiitd gksqdeveip arelrnvgve vfslgikaad akelkqiast pslnhvfnva
      301 nfdaivdiqn eiisqvcsgv deqlgelvsg eevveppsnl iamevsskyv klnwnpspsp
      361 vtgykviltp mtagsrqhal svgpqtttls vrdlsadtey qisvsamkgm tssepisime
      421 ktqpmkvqve csrgvdikad ivflvdgsys igianfvkvr aflevlvksf eispnrvqis
      481 lvqysrdpht eftlkkftkv ediieaintf pyrggstntg kamtyvreki fvpskgsrsn
      541 vpkvmilitd gkssdafrdp aiklrnsdve ifavgvkdav rseleaiasp paethvftve
      601 dfdafqrisf eltqsiclri eqelaaikkk ayvppkdlsf sevtsygfkt nwspagenvf
      661 syhitykeaa gddevtvvep asstsvvlss lkpetlylvn vtaeyedgfs iplageette
      721 evkgaprnlk vtdettdsfk itwtqapgrv lryriiyrpv aggesrevtt ppnqrrrtle
      781 nlipdtkyev svipeyfsgp gtpltgnaat eevrgnprdl rvsdpttstm klswsgapgk
      841 vkqylvtytp vaggetqevt vrgdttntvl qglkegtqya lsvtalyasg agdalfgegt
      901 tleergspqd lvtkditdts igaywtsapg mvrgyrvswk slyddvdtge knlpedaiht
      961 mienlqpetk yrisvfatys sgegepltgd attelsqdsk tlkvdeeten tmrvtwkpap
     1021 gkvvnyrvvy rphgrgkqmv akvpptvtst vlkrlqpqtt yditvlpiyk mgegklrqgs
     1081 gttasrfksp rnlktsdptm ssfrvtwepa pgevkgykvt fhptgddrrl gelvvgpydn
     1141 tvvleelrag ttykvnvfgm fdggessplv gqemttlsdt tvmpilssgm ecltraeadi
     1201 vllvdgswsi granfrtvrs fisrivevfd igpkrvqial aqysgdprte wqlnahrdkk
     1261 sllqavanlp ykggntltgm alnfirqqnf rtqagmrpra rkigvlitdg ksqddveaps
     1321 kklkdegvel faigiknade velkmiatdp ddthaynvad feslsrivdd ltinlcnsvk
     1381 gpgdleapsn lviserthrs frvswtppsd svdrykveyy pvsggkrqef yvsrmetstv
     1441 lkdlkpetey vvnvysvved eyseplkgte ktlpvpvvsl niydvgpttm hvqwqpvgga
     1501 tgyilsykpv kdteptrpke vrlgptvndm qltdlvpnte yavtvqavlh dltsepvtvr
     1561 evtlplprpq dlklrdvths tmnvfwepvp gkvrkyivry ktpeedvkev evdrsetsts
     1621 lkdlfsqtly tvsvsavhde gesppvtaqe ttrpvpaptn lkitevtseg frgtwdhgas
     1681 dvslyritwa pfgssdkmet ilngdentlv fenlnpntiy evsitaiypd esesddligs
     1741 ertlpilttq apksgprnlq vynatsnslt vkwdpasgrv qkyrityqps tgegneqttt
     1801 iggrqnsvvl qklkpdtpyt itvsslypdg eggrmtgrgk tkplntvrnl rvydpststl
     1861 nvrwdhaegn prqyklfyap aaggpeelvp ipgntnyail rnlqpdtsyt vtvvpvyteg
     1921 dggrtsdtgr tlmrglarnv qvynptpnsl dvrwdpapgp vlqyrvvysp vdgtrpsesi
     1981 vvpgntrmvh lerlipdtly svnlvalysd gegnpspaqg rtlprsgprn lrvfgettns
     2041 lsvawdhadg pvqqyriiys ptvgdpidey ttvpgrrnnv ilqplqpdtp ykitviavye
     2101 dgdgghltgn grtvgllppq nihisdewyt rfrvswdpsp spvlgykivy kpvgsnepme
     2161 afvgemtsyt lhnlnpstty dvnvyaqyds glsvpltdqg ttlylnvtdl ktyqigwdtf
     2221 cvkwsphraa tsyrlklspa dgtrgqeitv rgsetshcft glspdtdygv tvfvqtpnle
     2281 gpgvsvkeht tvkpteapte pptpppppti ppardvckga kadivfltda swsigddnfn
     2341 kvvkfifntv ggfdeispag iqvsfvqysd evksefklnt yndkalalga lqniryrggn
     2401 trtgkaltfi kekvltwesg mrknvpkvlv vvtdgrsqde vkkaalviqq sgfsvfvvgv
     2461 advdynelan iaskpserhv fivddfesfe kiednlitfv cetatsscpl iyldgytspg
     2521 fkmleaynlt eknfasvqgv slesgsfpsy sayriqknaf vnqptadlhp nglppsytii
     2581 llfrllpetp sdpfaiwqit drdykpqvgv iadpssktls ffnkdtrgev qtvtfdteev
     2641 ktlfygsfhk vhivvtsksv kiyidcyeii ekdikeagni ttdgyeilgk llkgerksaa
     2701 fqiqsfdivc spvwtsrdrc cdipsrrdeg kcpafpnsct ctqdsvgppg ppgpaggpga
     2761 kgprgergis gaigppgprg digppgpqgp pgpqgpngls ipgeqgrqgm kgdagepglp
     2821 grtgtpglpg ppgpmgppgd rgftgkdgam gprgppgppg spgspgvtgp sgkpgkpgdh
     2881 grpgpsglkg ekgdrgdias qnmmravarq vceqlisgqm nrfnqmlnqi pndyqssrnq
     2941 pgppgppgpp gsagargepg pggrpgfpgt pgmqgppger glpgekgerg tgssgprglp
     3001 gppgpqgesr tgppgstgsr gppgppgrpg nsgirgppgp pgycdssqca sipyngqgyp
     3061 gsg
//
