LOCUS       NP_005325               2035 aa            linear   PRI 27-APR-2025
DEFINITION  host cell factor 1 isoform 2 [Homo sapiens].
ACCESSION   NP_005325
VERSION     NP_005325.2
DBSOURCE    REFSEQ: accession NM_005334.3
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 2035)
  AUTHORS   Hussain,S.I., Muhammad,N., Shah,S.A., Rehman,A.U., Khan,S.A.,
            Saleha,S., Khan,Y.M., Muhammad,N., Khan,S. and Wasif,N.
  TITLE     Variants in HCFC1 and MN1 genes causing intellectual disability in
            two Pakistani families
  JOURNAL   BMC Med Genomics 17 (1), 176 (2024)
   PUBMED   38956580
  REMARK    GeneRIF: Variants in HCFC1 and MN1 genes causing intellectual
            disability in two Pakistani families.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2035)
  AUTHORS   He,N., Guan,B.Z., Wang,J., Liu,H.K., Mao,Y., Liu,Z.G., Yin,F.,
            Peng,J., Xiao,B., Tang,B.S., Zhou,D., Huang,G., Dai,Q.L., Zeng,Y.,
            Han,H., Zhai,Q.X., Li,B., Tang,B., Li,W.B., Song,W., Liu,L.,
            Shi,Y.W., Li,B.M., Su,T., Zhou,P., Liu,X.R., Guo,L.W., Yi,Y.H. and
            Liao,W.P.
  TITLE     HCFC1 variants in the proteolysis domain are associated with
            X-linked idiopathic partial epilepsy: Exploring the underlying
            mechanism
  JOURNAL   Clin Transl Med 13 (6), e1289 (2023)
   PUBMED   37264743
  REMARK    GeneRIF: HCFC1 variants in the proteolysis domain are associated
            with X-linked idiopathic partial epilepsy: Exploring the underlying
            mechanism.
REFERENCE   3  (residues 1 to 2035)
  AUTHORS   Wongkittichote,P., Wegner,D.J. and Shinawi,M.S.
  TITLE     Novel exon-skipping variant disrupting the basic domain of HCFC1
            causes intellectual disability without metabolic abnormalities in
            both male and female patients
  JOURNAL   J Hum Genet 66 (7), 717-724 (2021)
   PUBMED   33517344
  REMARK    GeneRIF: Novel exon-skipping variant disrupting the basic domain of
            HCFC1 causes intellectual disability without metabolic
            abnormalities in both male and female patients.
REFERENCE   4  (residues 1 to 2035)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 2035)
  AUTHORS   Xiang,P., Li,F., Ma,Z., Yue,J., Lu,C., You,Y., Hou,L., Yin,B.,
            Qiang,B., Shu,P. and Peng,X.
  TITLE     HCF-1 promotes cell cycle progression by regulating the expression
            of CDC42
  JOURNAL   Cell Death Dis 11 (10), 907 (2020)
   PUBMED   33097698
  REMARK    GeneRIF: HCF-1 promotes cell cycle progression by regulating the
            expression of CDC42.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 2035)
  AUTHORS   Wilson,A.C., Peterson,M.G. and Herr,W.
  TITLE     The HCF repeat is an unusual proteolytic cleavage signal
  JOURNAL   Genes Dev 9 (20), 2445-2458 (1995)
   PUBMED   7590226
REFERENCE   7  (residues 1 to 2035)
  AUTHORS   Frattini,A., Faranda,S., Redolfi,E., Zucchi,I., Villa,A.,
            Patrosso,M.C., Strina,D., Susani,L. and Vezzoni,P.
  TITLE     Genomic organization of the human VP16 accessory protein, a
            housekeeping gene (HCFC1) mapping to Xq28
  JOURNAL   Genomics 23 (1), 30-35 (1994)
   PUBMED   7829097
REFERENCE   8  (residues 1 to 2035)
  AUTHORS   Sloan,J.L., Carrillo,N., Adams,D. and Venditti,C.P.
  TITLE     Disorders of Intracellular Cobalamin Metabolism
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301503
REFERENCE   9  (residues 1 to 2035)
  AUTHORS   Mulley,J.C., Kerr,B., Stevenson,R. and Lubs,H.
  TITLE     Nomenclature guidelines for X-linked mental retardation
  JOURNAL   Am J Med Genet 43 (1-2), 383-391 (1992)
   PUBMED   1605216
  REMARK    Review article
REFERENCE   10 (residues 1 to 2035)
  AUTHORS   Gedeon,A., Kerr,B., Mulley,J. and Turner,G.
  TITLE     Localisation of the MRX3 gene for non-specific X linked mental
            retardation
  JOURNAL   J Med Genet 28 (6), 372-377 (1991)
   PUBMED   1870093
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U52112.2, BC063435.1, L20010.1
            and BC010606.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 19, 2006 this sequence version replaced NP_005325.1.
            
            Summary: This gene is a member of the host cell factor family and
            encodes a protein with five Kelch repeats, a fibronectin-like
            motif, and six HCF repeats, each of which contains a highly
            specific cleavage signal. This nuclear coactivator is
            proteolytically cleaved at one of the six possible sites, resulting
            in the creation of an N-terminal chain and the corresponding
            C-terminal chain. The final form of this protein consists of
            noncovalently bound N- and C-terminal chains. The protein is
            involved in control of the cell cycle and transcriptional
            regulation during herpes simplex virus infection. Alternatively
            spliced variants which encode different protein isoforms have been
            described; however, not all variants have been fully characterized.
            [provided by RefSeq, Jul 2008].
            
            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 :: L20010.1, SRR11853560.30529.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000310441.12/ ENSP00000309555.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2035
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..2035
                     /product="host cell factor 1 isoform 2"
                     /note="host cell factor 1; VP16-accessory protein; protein
                     phosphatase 1, regulatory subunit 89"
                     /calculated_mol_wt=208602
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Region          25..344
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          33..80
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          44..89
                     /region_name="Kelch 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Region          84..134
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          93..140
                     /region_name="Kelch 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Region          137..196
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          148..194
                     /region_name="Kelch 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Region          200..253
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          217..265
                     /region_name="Kelch 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Region          255..319
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          266..313
                     /region_name="Kelch 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Site            288
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     Region          322..367
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          407..434
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     Region          <466..771
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          500..550
                     /region_name="Required for interaction with OGT.
                     /evidence=ECO:0000269|PubMed:21285374"
                     /note="propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Site            504
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     Site            524
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     Region          610..722
                     /region_name="Interaction with SIN3A.
                     /evidence=ECO:0000269|PubMed:12670868"
                     /note="propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Site            666
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     Site            669
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     Region          750..902
                     /region_name="Interaction with ZBTB17.
                     /evidence=ECO:0000269|PubMed:12244100"
                     /note="propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Region          813..912
                     /region_name="Interaction with GABP2.
                     /evidence=ECO:0000269|PubMed:10675337"
                     /note="propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Site            813
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     Region          1010..1035
                     /region_name="HCF repeat 1.
                     /evidence=ECO:0000305|PubMed:7590226"
                     /note="propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Site            1019..1020
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:7590226; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     Region          1072..1097
                     /region_name="HCF repeat 2.
                     /evidence=ECO:0000305|PubMed:7590226"
                     /note="propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Site            1081..1082
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:7590226; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     Region          1101..1126
                     /region_name="HCF repeat 3.
                     /evidence=ECO:0000305|PubMed:7590226"
                     /note="propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Site            1110..1111
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000305|PubMed:7590226; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     Region          1158..1183
                     /region_name="HCF repeat 4, degenerate.
                     /evidence=ECO:0000305|PubMed:7590226"
                     /note="propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Site            1205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     Site            1219
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     Site            1224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     Region          1286..1311
                     /region_name="HCF repeat 5.
                     /evidence=ECO:0000305|PubMed:7590226"
                     /note="propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Region          1292..1371
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Site            1295..1296
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000305|PubMed:7590226; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     Site            1323..1324
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:10920196,
                     ECO:0000305|PubMed:7590226; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     Region          1349..1374
                     /region_name="HCF repeat 7, degenerate.
                     /evidence=ECO:0000305|PubMed:7590226"
                     /note="propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Region          1414..1439
                     /region_name="HCF repeat 8.
                     /evidence=ECO:0000305|PubMed:7590226"
                     /note="propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Site            1423..1424
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:10920196,
                     ECO:0000305|PubMed:7590226; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     Region          1435..1470
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Region          1487..1515
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Site            1491
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     Site            1497
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     Site            1507
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     Site            1771
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     Site            1838
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61191; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     Region          <1856..1885
                     /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(1874..1875,1877..1878)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          1891..1996
                     /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(1891,1969,1990)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(1991..1992,1994..1995)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          1994..2035
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51610.2)"
     Site            2005
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P51610.2)"
     CDS             1..2035
                     /gene="HCFC1"
                     /gene_synonym="CFF; HCF; HCF-1; HCF1; HFC1; MAHCX; MRX3;
                     PPP1R89; VCAF; XLID3"
                     /coded_by="NM_005334.3:979..7086"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS44020.1"
                     /db_xref="GeneID:3054"
                     /db_xref="HGNC:HGNC:4839"
                     /db_xref="MIM:300019"
ORIGIN      
        1 masavspanl pavllqprwk rvvgwsgpvp rprhghrava ikelivvfgg gnegivdelh
       61 vyntatnqwf ipavrgdipp gcaaygfvcd gtrllvfggm veygkysndl yelqasrwew
      121 krlkaktpkn gpppcprlgh sfslvgnkcy lfgglandse dpknnipryl ndlyilelrp
      181 gsgvvawdip itygvlpppr eshtavvyte kdnkksklvi yggmsgcrlg dlwtldidtl
      241 twnkpslsgv aplprslhsa ttignkmyvf ggwvplvmdd vkvathekew kctntlacln
      301 ldtmawetil mdtlednipr araghcavai ntrlyiwsgr dgyrkawnnq vcckdlwyle
      361 tekpppparv qlvrantnsl evswgavata dsyllqlqky dipataatat sptpnpvpsv
      421 panppkspap aaaapavqpl tqvgitllpq aapapptttt iqvlptvpgs sisvptaart
      481 qgvpavlkvt gpqattgtpl vtmrpasqag kapvtvtslp agvrmvvptq saqgtvigss
      541 pqmsgmaala aaaaatqkip pssaptvlsv pagttivktm avtpgtttlp atvkvasspv
      601 mvsnpatrml ktaaaqvgts vssatntstr piitvhksgt vtvaqqaqvv ttvvggvtkt
      661 itlvkspisv pggsalisnl gkvmsvvqtk pvqtsavtgq astgpvtqii qtkgplpagt
      721 ilklvtsadg kpttiitttq asgagtkpti lgissvspst tkpgtttiik tipmsaiitq
      781 agatgvtssp gikspitiit tkvmtsgtga pakiitavpk iatghgqqgv tqvvlkgapg
      841 qpgtilrtvp mggvrlvtpv tvsavkpavt tlvvkgttgv ttlgtvtgtv stslagaggh
      901 stsaslatpi ttlgtiatls sqvinptait vsaaqttlta agglttptit mqpvsqptqv
      961 tlitapsgve aqpvhdlpvs ilasptteqp tatvtiadsg qgdvqpgtvt lvcsnppcet
     1021 hetgttntat ttvvanlggh pqptqvqfvc drqeaaaslv tstvgqqngs vvrvcsnppc
     1081 ethetgttnt attatsnmag qhgcsnppce thetgttnta ttamssvgan hqrdarraca
     1141 agtpaviris vatgaleaaq gsksqcqtrq tsatsttmtv matgapcsag pllgpsmare
     1201 pggrspafvq laplsskvrl sspsikdlpa grhshavsta amtrssvgag eprmapvces
     1261 lqggspsttv tvtaleallc psatvtqvcs nppcethetg ttntattsna gsaqrvcsnp
     1321 pcethetgtt htattatsng gtgqpeggqq ppagrpceth qttstgttms vsvgallpda
     1381 tsshrtvesg levaaapsvt pqagtallap fptqrvcsnp pcethetgtt htattvtsnm
     1441 ssnqdpppaa sdqgevestq gdsvnitsss aitttvsstl travttvtqs tpvpgpsvpp
     1501 peelqvspgp rqqlpprqll qsastalmge saevlsasqt pelpaavdls stgepssgqe
     1561 sagsavvatv vvqpppptqs evdqlslpqe lmaeaqagtt tlmvtgltpe elavtaaaea
     1621 aaqaaateea qalaiqavlq aaqqavmgtg epmdtseaaa tvtqaelghl saegqegqat
     1681 tipivltqqe laalvqqqql qeaqaqqqhh hlptealapa dslndpaies nclnelagtv
     1741 pstvallpst ateslapsnt fvapqpvvva spaklqaaat ltevangies lgvkpdlppp
     1801 pskapmkken qwfdvgvikg tnvmvthyfl ppddavpsdd dlgtvpdynq lkkqelqpgt
     1861 aykfrvagin acgrgpfsei safktclpgf pgapcaikis kspdgahltw eppsvtsgki
     1921 ieysvylaiq ssqaggelks stpaqlafmr vycgpspscl vqssslsnah idyttkpaii
     1981 friaarnekg ygpatqvrwl qetskdssgt kpankrpmss pemksapkks kadgq
//
