ID I3M556_ICTTR Unreviewed; 760 AA.
AC I3M556;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Fibroblast activation protein alpha {ECO:0000313|Ensembl:ENSSTOP00000004433.2};
GN Name=FAP {ECO:0000313|Ensembl:ENSSTOP00000004433.2};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000004433.2, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000004433.2}
RP IDENTIFICATION.
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; AGTP01000299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01000300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3M556; -.
DR STRING; 43179.ENSSTOP00000004433; -.
DR MEROPS; S09.007; -.
DR GlyCosmos; I3M556; 6 sites, No reported glycans.
DR Ensembl; ENSSTOT00000004941.3; ENSSTOP00000004433.2; ENSSTOG00000004923.3.
DR eggNOG; KOG2100; Eukaryota.
DR GeneTree; ENSGT00940000160454; -.
DR HOGENOM; CLU_006105_4_3_1; -.
DR InParanoid; I3M556; -.
DR OMA; MRTPQEN; -.
DR OrthoDB; 2876738at2759; -.
DR TreeFam; TF313309; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0045178; C:basal part of cell; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1905368; C:peptidase complex; IEA:Ensembl.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:Ensembl.
DR GO; GO:0043542; P:endothelial cell migration; IEA:Ensembl.
DR GO; GO:1902362; P:melanocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0097325; P:melanocyte proliferation; IEA:Ensembl.
DR GO; GO:0060244; P:negative regulation of cell proliferation involved in contact inhibition; IEA:Ensembl.
DR GO; GO:0010716; P:negative regulation of extracellular matrix disassembly; IEA:Ensembl.
DR GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IEA:Ensembl.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0010710; P:regulation of collagen catabolic process; IEA:Ensembl.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
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:UP000005215}.
FT DOMAIN 106..472
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 555..757
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 760 AA; 87723 MW; D5FF24F54FE5AD3E CRC64;
MKTWLKIVFG VATSAVLALL VMCIVLRPSR VHNPEGSTKR ALTLKDILNG TFSYKTFFPN
WISGQEYLHQ STENNIILYN IETGESYIIL SNSTMKSVNA SNYGLSPDRQ FAYLESDYSK
LWRYSYTATY HIYDLINGEF VKGYELPRPI QYLCWSPVGS KLVYVYQNNI YLKQRPGDPP
FQITYNGKKN KIFNGIPDWV YEEEMLATKY ALWWSPNGKF LAYAEFNDTD IPVIAYSYYG
DEQYPRTINI PYPKAGAKNP IVRIFIIDTT YPQHVGPREV PVPAMIASSD YYFSWLTWVN
DERICLQWLK RVQNVSVLSI CDFREDWQIW DCPKTQEHIE ESRTGWAGGF FVSTPVFSYD
AISYYKIFSD KDGYKHIHYI KDSVENAIQI TSGKWEAINI FRVTQDSLFY SSNEFEGYPG
RRNIYRISIG SYPPSKKCVT CHLRKERCQY YTASFSDYAK YYALICYGPG LPISTLHDGR
TDQEIKILEE NKELENALKN IQLPKEEIKK LEVDEITLWY KMILPPQFDR SKKYPLLIQV
YGGPCSQSVR SVFAVNWISY LSSKEGMVIA LVDGRGTAFQ GDKLLYAVYR KLGVYEVEDQ
ITAVRKFIEM GFIDEKRIAI WGWSYGGYVS SLALASGTGL FKCGIAVAPV SSWEYYASIY
TERFMGFPTK DDNLEHYKNS TVMARAEYFR NVDYLLIHGT ADDNVHFQNS AQIAKALVNA
QVDFQAMWYS DQNHGLSGLS TNHLYTHMTH FLKQCFSSSD
//
