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Fibroblast activation protein, alpha

 F1LMH7_RAT              Unreviewed;       760 AA.
F1LMH7;
03-MAY-2011, integrated into UniProtKB/TrEMBL.
22-JUL-2015, sequence version 3.
28-MAR-2018, entry version 48.
SubName: Full=Fibroblast activation protein, alpha {ECO:0000313|Ensembl:ENSRNOP00000008148};
Name=Fap {ECO:0000313|Ensembl:ENSRNOP00000008148,
ECO:0000313|RGD:621253};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000008148, ECO:0000313|Proteomes:UP000002494};
[1] {ECO:0000313|Ensembl:ENSRNOP00000008148, ECO:0000313|Proteomes:UP000002494}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000008148,
ECO:0000313|Proteomes:UP000002494};
PubMed=15057822; DOI=10.1038/nature02426;
Rat Genome Sequencing Project Consortium;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2] {ECO:0000313|Ensembl:ENSRNOP00000008148}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000008148};
Ensembl;
Submitted (JUL-2011) to UniProtKB.
-!- SIMILARITY: Belongs to the peptidase S9B family.
{ECO:0000256|SAAS:SAAS01028250}.
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EMBL; AABR07052347; -; NOT_ANNOTATED_CDS; Genomic_DNA.
STRING; 10116.ENSRNOP00000008148; -.
ESTHER; ratno-FAP; DPP4N_Peptidase_S9.
PaxDb; F1LMH7; -.
PRIDE; F1LMH7; -.
Ensembl; ENSRNOT00000008148; ENSRNOP00000008148; ENSRNOG00000005679.
RGD; 621253; Fap.
eggNOG; KOG2100; Eukaryota.
eggNOG; COG1506; LUCA.
GeneTree; ENSGT00760000119233; -.
InParanoid; F1LMH7; -.
OMA; NEFEGYP; -.
OrthoDB; EOG091G0BU5; -.
TreeFam; TF313309; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000005679; -.
ExpressionAtlas; F1LMH7; baseline and differential.
GO; GO:0045177; C:apical part of cell; ISO:RGD.
GO; GO:0045178; C:basal part of cell; ISO:RGD.
GO; GO:0009986; C:cell surface; ISO:RGD.
GO; GO:0005615; C:extracellular space; ISO:RGD.
GO; GO:0005925; C:focal adhesion; ISO:RGD.
GO; GO:0071438; C:invadopodium membrane; ISO:RGD.
GO; GO:0030027; C:lamellipodium; ISO:RGD.
GO; GO:0005886; C:plasma membrane; ISO:RGD.
GO; GO:0008239; F:dipeptidyl-peptidase activity; ISO:RGD.
GO; GO:0004175; F:endopeptidase activity; ISO:RGD.
GO; GO:0005178; F:integrin binding; ISO:RGD.
GO; GO:0008233; F:peptidase activity; ISO:RGD.
GO; GO:0002020; F:protease binding; ISO:RGD.
GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
GO; GO:0004252; F:serine-type endopeptidase activity; ISO:RGD.
GO; GO:0008236; F:serine-type peptidase activity; ISO:RGD.
GO; GO:0043542; P:endothelial cell migration; ISO:RGD.
GO; GO:1902362; P:melanocyte apoptotic process; ISO:RGD.
GO; GO:0097325; P:melanocyte proliferation; ISO:RGD.
GO; GO:0071850; P:mitotic cell cycle arrest; ISO:RGD.
GO; GO:0060244; P:negative regulation of cell proliferation involved in contact inhibition; ISO:RGD.
GO; GO:0010716; P:negative regulation of extracellular matrix disassembly; ISO:RGD.
GO; GO:1903054; P:negative regulation of extracellular matrix organization; ISO:RGD.
GO; GO:0071158; P:positive regulation of cell cycle arrest; ISO:RGD.
GO; GO:1900119; P:positive regulation of execution phase of apoptosis; ISO:RGD.
GO; GO:0006508; P:proteolysis; ISO:RGD.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; ISO:RGD.
GO; GO:0010710; P:regulation of collagen catabolic process; ISO:RGD.
Gene3D; 2.140.10.30; -; 1.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR031245; FAP/Dpf2.
InterPro; IPR002471; Pept_S9_AS.
InterPro; IPR001375; Peptidase_S9.
InterPro; IPR002469; Peptidase_S9B_N.
InterPro; IPR038554; Peptidase_S9B_N_sf.
PANTHER; PTHR11731:SF136; PTHR11731:SF136; 1.
Pfam; PF00930; DPPIV_N; 1.
Pfam; PF00326; Peptidase_S9; 1.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
3: Inferred from homology;
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000002494};
Reference proteome {ECO:0000313|Proteomes:UP000002494}.
DOMAIN 105 471 DPPIV_N. {ECO:0000259|Pfam:PF00930}.
DOMAIN 553 757 Peptidase_S9. {ECO:0000259|Pfam:PF00326}.
COILED 479 499 {ECO:0000256|SAM:Coils}.
SEQUENCE 760 AA; 87715 MW; AFCD3DE7F8DFD6DC CRC64;
MTWLKTVFGV TTLVALALVV ICIVLRPSRV YSPEGNTGRS LTLKDILNGT FSYKTYFPNW
ISEQEYLHQS EDDNIVFYNI ETRESYIILS NSTMKSVNAT DYGLSPDRQF IYLESDYSKL
WRYSYTATYY IYDLQNGEFV RGYELPRPIQ YLCWSPVGSK LAYVYQNNIY LKQRPGDPPF
QITYTGRENR IFNGIPDWVY EEEMLATKYA LWWSPDGKYL AYVEFNDSDI PIIAYSYYGD
GQYPRTINIP YPKAGAKNPI VRVFIVDTIY PHHVGPIEVP VPEMIASSDY YFTWLTWVTN
ERVCLQWLKR VQNVSVLSIC DFREDWHAWD CPKNQEHIEE SRTGWAGGFF VSTPAFSQDA
ASYYKIFSDK DGYKHIHYIK DTVENAIQIT SGKWEAIYIF RVTQDSLFYS SNEFEGYPGR
RNIYRISIGN SPPSKKCVTC HLRKERCQYY TASFSYKAKY YALICYGPGL PISTLHDGRT
DQEIQVLEEN KELENALRNI QLPAVEIKKL EDGGMTFWYK MILPPQFDRS KKYPLLIQVY
GGPCSQSVKS VFSVNWITYL ASKEGIVVAL VDGRGTAFQG DKFLHAVYRK LGVYEVEDQL
TAVRKFIEMG FIDEGRIAIW GWSYGGYVSS LALASGTGLF KCGIAVAPVS SWEYYASIYT
ERFMGLPTKD DNLEHYKNST VMARAEYFRN VDYLLIHGTA DDNVHFQNSA QIAKALVNAQ
VDFQAMWYSD QNHGISSGRS QNHLYTHMTH FLKQCFSLSD


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