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Database: UniProt
Entry: A0A286XTM5_CAVPO
LinkDB: A0A286XTM5_CAVPO
Original site: A0A286XTM5_CAVPO 
ID   A0A286XTM5_CAVPO        Unreviewed;       692 AA.
AC   A0A286XTM5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Fibroblast activation protein alpha {ECO:0000313|Ensembl:ENSCPOP00000028876.1};
GN   Name=FAP {ECO:0000313|Ensembl:ENSCPOP00000028876.1};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000028876.1, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000028876.1}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000028876.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC       Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC       Cell projection, invadopodium membrane {ECO:0000256|ARBA:ARBA00004341};
CC       Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004341}.
CC       Cell projection, lamellipodium membrane
CC       {ECO:0000256|ARBA:ARBA00004485}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004485}.
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DR   EMBL; AAKN02005855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02005856; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A286XTM5; -.
DR   GlyCosmos; A0A286XTM5; 5 sites, No reported glycans.
DR   Ensembl; ENSCPOT00000037887.1; ENSCPOP00000028876.1; ENSCPOG00000011995.4.
DR   VEuPathDB; HostDB:ENSCPOG00000011995; -.
DR   GeneTree; ENSGT00940000160454; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000011995; Expressed in zone of skin and 6 other cell types or tissues.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 2.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   PANTHER; PTHR11731:SF136; PROLYL ENDOPEPTIDASE FAP; 1.
DR   PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   4: Predicted;
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..692
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012222571"
FT   DOMAIN          73..221
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          486..689
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   692 AA;  80113 MW;  144A5F867E564E2B CRC64;
     MKTWLKIVFG ITTSALLALL MVCIVLNPSR GEEYLHQSTD DNVILYNIET GESYTILSNS
     TMKSVNASNY GLSPDRQFAY LESDYSKLWR YSYTATYHIY DLRNGEFLKG YELPRPIQYL
     SWSPVGSKLA YVYQNNIYLK QRPEDPPFQV TYNGKENKIF NGIPDWVYEE EMLGTKYALW
     WSPNGNFLAY AEFNDTDIPV IAYSYYGDEQ YPRIINIPYP KDYYFTWLTW VTDDRVCVQW
     LKRVQNVSVL SICDFREDWN TWDCPKAQEH VEESRSGWAG GFFVSAPTFS YDSISYYKIF
     SDKDGYKHIH YIKDTVENAI QITSGKWEAI NILRVTQDSL FYSSNEFEGY PGRKNIYRIS
     IGSYPPSKKC VTCHLRKERC QYYTASFSYY AKYYALICYG PGLPISTLHD GRTDQEIKIL
     EDNKELENAL KHIQLPKEEI KKLEVDEITL WYKMILPPQF DRSKKYPLLI QVYGGPCTQS
     VKSIFSINWI SYLASKEDIV IALVDGRGTA FQGDKILYAV YRKLGVYEVE DQITAVRKFI
     EMGFIDEKRI AIWGWSYGGY VSSLTLASGS GLFKCGIAVA PVSSWEYYAS IYTERFMGLP
     TKDDNLAHYK NSTVMARAEY FRNVDYLLIH GTADDNVHFQ NSAQIAKALV NAQVDFQAMW
     YSDQNHGISG ISTNHLYTHM THFLKQCFSS SD
//
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