LOCUS       NP_004451                760 aa            linear   PRI 03-SEP-2024
DEFINITION  prolyl endopeptidase FAP isoform 1 [Homo sapiens].
ACCESSION   NP_004451
VERSION     NP_004451.2
DBSOURCE    REFSEQ: accession NM_004460.5
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 760)
  AUTHORS   Oguri,N., Gi,T., Nakamura,E., Furukoji,E., Goto,H., Maekawa,K.,
            Tsuji,A.B., Nishii,R., Aman,M., Moriguchi-Goto,S., Sakae,T.,
            Azuma,M. and Yamashita,A.
  TITLE     Expression of fibroblast activation protein-alpha in human deep
            vein thrombosis
  JOURNAL   Thromb Res 241, 109075 (2024)
   PUBMED   38955058
  REMARK    GeneRIF: Expression of fibroblast activation protein-alpha in human
            deep vein thrombosis.
REFERENCE   2  (residues 1 to 760)
  AUTHORS   Xu,S., Jiemy,W.F., Boots,A.M.H., Arends,S., van Sleen,Y.,
            Nienhuis,P.H., van der Geest,K.S.M., Heeringa,P., Brouwer,E. and
            Sandovici,M.
  TITLE     Altered Plasma Levels and Tissue Expression of Fibroblast
            Activation Protein Alpha in Giant Cell Arteritis
  JOURNAL   Arthritis Care Res (Hoboken) 76 (9), 1322-1332 (2024)
   PUBMED   38685696
  REMARK    GeneRIF: Altered Plasma Levels and Tissue Expression of Fibroblast
            Activation Protein Alpha in Giant Cell Arteritis.
REFERENCE   3  (residues 1 to 760)
  AUTHORS   Li,R., Zhang,R., Shi,X., Jiao,X., Li,Y., Zhao,Y., Liu,T. and
            Zhang,C.
  TITLE     Expression of FAP in Oral Leukoplakia and Oral Squamous Cell
            Carcinoma
  JOURNAL   Int Dent J 74 (3), 581-588 (2024)
   PUBMED   38278714
  REMARK    GeneRIF: Expression of FAP in Oral Leukoplakia and Oral Squamous
            Cell Carcinoma.
REFERENCE   4  (residues 1 to 760)
  AUTHORS   Engquist,E.N., Greco,A., Joosten,L.A.B., van Engelen,B.G.M.,
            Zammit,P.S. and Banerji,C.R.S.
  TITLE     FSHD muscle shows perturbation in fibroadipogenic progenitor cells,
            mitochondrial function and alternative splicing independently of
            inflammation
  JOURNAL   Hum Mol Genet 33 (2), 182-197 (2024)
   PUBMED   37856562
  REMARK    GeneRIF: FSHD muscle shows perturbation in fibroadipogenic
            progenitor cells, mitochondrial function and alternative splicing
            independently of inflammation.
REFERENCE   5  (residues 1 to 760)
  AUTHORS   Wu,Y., Wu,C., Shi,T., Cai,Q., Wang,T., Xiong,Y., Zhang,Y.,
            Jiang,W., Lu,M., Chen,Z., Chen,J., Wang,J. and He,R.
  TITLE     FAP expression in adipose tissue macrophages promotes obesity and
            metabolic inflammation
  JOURNAL   Proc Natl Acad Sci U S A 120 (51), e2303075120 (2023)
   PUBMED   38100414
  REMARK    GeneRIF: FAP expression in adipose tissue macrophages promotes
            obesity and metabolic inflammation.
REFERENCE   6  (residues 1 to 760)
  AUTHORS   Niedermeyer,J., Enenkel,B., Park,J.E., Lenter,M., Rettig,W.J.,
            Damm,K. and Schnapp,A.
  TITLE     Mouse fibroblast-activation protein--conserved Fap gene
            organization and biochemical function as a serine protease
  JOURNAL   Eur J Biochem 254 (3), 650-654 (1998)
   PUBMED   9688278
REFERENCE   7  (residues 1 to 760)
  AUTHORS   Goldstein,L.A., Ghersi,G., Pineiro-Sanchez,M.L., Salamone,M.,
            Yeh,Y., Flessate,D. and Chen,W.T.
  TITLE     Molecular cloning of seprase: a serine integral membrane protease
            from human melanoma
  JOURNAL   Biochim Biophys Acta 1361 (1), 11-19 (1997)
   PUBMED   9247085
REFERENCE   8  (residues 1 to 760)
  AUTHORS   Pineiro-Sanchez,M.L., Goldstein,L.A., Dodt,J., Howard,L., Yeh,Y.,
            Tran,H., Argraves,W.S. and Chen,W.T.
  TITLE     Identification of the 170-kDa melanoma membrane-bound gelatinase
            (seprase) as a serine integral membrane protease
  JOURNAL   J Biol Chem 272 (12), 7595-7601 (1997)
   PUBMED   9065413
  REMARK    Erratum:[J Biol Chem. 1998 May 22:273(21):13366]
REFERENCE   9  (residues 1 to 760)
  AUTHORS   Rettig,W.J., Su,S.L., Fortunato,S.R., Scanlan,M.J., Raj,B.K.,
            Garin-Chesa,P., Healey,J.H. and Old,L.J.
  TITLE     Fibroblast activation protein: purification, epitope mapping and
            induction by growth factors
  JOURNAL   Int J Cancer 58 (3), 385-392 (1994)
   PUBMED   7519584
REFERENCE   10 (residues 1 to 760)
  AUTHORS   Scanlan,M.J., Raj,B.K., Calvo,B., Garin-Chesa,P.,
            Sanz-Moncasi,M.P., Healey,J.H., Old,L.J. and Rettig,W.J.
  TITLE     Molecular cloning of fibroblast activation protein alpha, a member
            of the serine protease family selectively expressed in stromal
            fibroblasts of epithelial cancers
  JOURNAL   Proc Natl Acad Sci U S A 91 (12), 5657-5661 (1994)
   PUBMED   7911242
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U09278.2, BC026250.1 and
            AL832166.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 15, 2001 this sequence version replaced NP_004451.1.
            
            Summary: The protein encoded by this gene is a homodimeric integral
            membrane gelatinase belonging to the serine protease family. It is
            selectively expressed in reactive stromal fibroblasts of epithelial
            cancers, granulation tissue of healing wounds, and malignant cells
            of bone and soft tissue sarcomas. This protein is thought to be
            involved in the control of fibroblast growth or
            epithelial-mesenchymal interactions during development, tissue
            repair, and epithelial carcinogenesis. Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Apr 2014].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            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 :: U09278.2, BC026250.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000188790.9/ ENSP00000188790.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..760
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.2"
     Protein         1..760
                     /product="prolyl endopeptidase FAP isoform 1"
                     /EC_number="3.4.14.5"
                     /EC_number="3.4.21.26"
                     /note="integral membrane serine protease; seprase; 170 kDa
                     melanoma membrane-bound gelatinase; dipeptidyl peptidase
                     FAP; surface-expressed protease; post-proline cleaving
                     enzyme; gelatine degradation protease FAP; prolyl
                     endopeptidase FAP"
                     /calculated_mol_wt=87582
     Site            5..25
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12884.5)"
     Site            23..24
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000303|PubMed:14751930;
                     propagated from UniProtKB/Swiss-Prot (Q12884.5)"
     mat_peptide     24..760
                     /product="Antiplasmin-cleaving enzyme FAP, soluble form.
                     /evidence=ECO:0000303|PubMed:14751930. /id=PRO_0000430643"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12884.5)"
                     /calculated_mol_wt=85250
     Site            49
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498,
                     ECO:0000269|PubMed:15809306; propagated from
                     UniProtKB/Swiss-Prot (Q12884.5)"
     Site            92
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498,
                     ECO:0000269|PubMed:15809306; propagated from
                     UniProtKB/Swiss-Prot (Q12884.5)"
     Site            99
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498,
                     ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (Q12884.5)"
     Region          106..473
                     /region_name="DPPIV_N"
                     /note="Dipeptidyl peptidase IV (DPP IV) N-terminal region;
                     pfam00930"
                     /db_xref="CDD:395744"
     Site            227
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498,
                     ECO:0000269|PubMed:15809306, ECO:0000269|PubMed:16335952;
                     propagated from UniProtKB/Swiss-Prot (Q12884.5)"
     Site            314
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498,
                     ECO:0000269|PubMed:15809306; propagated from
                     UniProtKB/Swiss-Prot (Q12884.5)"
     Region          553..756
                     /region_name="Peptidase_S9"
                     /note="Prolyl oligopeptidase family; pfam00326"
                     /db_xref="CDD:459761"
     Site            679
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q12884.5)"
     CDS             1..760
                     /gene="FAP"
                     /gene_synonym="DPPIV; FAPA; FAPalpha; SIMP"
                     /coded_by="NM_004460.5:119..2401"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33311.1"
                     /db_xref="GeneID:2191"
                     /db_xref="HGNC:HGNC:3590"
                     /db_xref="MIM:600403"
ORIGIN      
        1 mktwvkivfg vatsavlall vmcivlrpsr vhnseentmr altlkdilng tfsyktffpn
       61 wisgqeylhq sadnnivlyn ietgqsytil snrtmksvna snyglspdrq fvylesdysk
      121 lwrysytaty yiydlsngef vrgnelprpi qylcwspvgs klayvyqnni ylkqrpgdpp
      181 fqitfngren kifngipdwv yeeemlatky alwwspngkf layaefndtd ipviaysyyg
      241 deqyprtini pypkagaknp vvrifiidtt ypayvgpqev pvpamiassd yyfswltwvt
      301 dervclqwlk rvqnvsvlsi cdfredwqtw dcpktqehie esrtgwaggf fvstpvfsyd
      361 aisyykifsd kdgykhihyi kdtvenaiqi tsgkweaini frvtqdslfy ssnefeeypg
      421 rrniyrisig syppskkcvt chlrkercqy ytasfsdyak yyalvcygpg ipistlhdgr
      481 tdqeikilee nkelenalkn iqlpkeeikk levdeitlwy kmilppqfdr skkyplliqv
      541 yggpcsqsvr svfavnwisy laskegmvia lvdgrgtafq gdkllyavyr klgvyevedq
      601 itavrkfiem gfidekriai wgwsyggyvs slalasgtgl fkcgiavapv ssweyyasvy
      661 terfmglptk ddnlehykns tvmaraeyfr nvdyllihgt addnvhfqns aqiakalvna
      721 qvdfqamwys dqnhglsgls tnhlythmth flkqcfslsd
//
