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Database: UniProt
Entry: H2QKV6_PANTR
LinkDB: H2QKV6_PANTR
Original site: H2QKV6_PANTR 
ID   H2QKV6_PANTR            Unreviewed;      1019 AA.
AC   H2QKV6;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   08-MAY-2019, entry version 60.
DE   RecName: Full=Enteropeptidase {ECO:0000256|PIRNR:PIRNR001138};
DE            EC=3.4.21.9 {ECO:0000256|PIRNR:PIRNR001138};
DE   AltName: Full=Enterokinase {ECO:0000256|PIRNR:PIRNR001138};
DE   AltName: Full=Serine protease 7 {ECO:0000256|PIRNR:PIRNR001138};
DE   AltName: Full=Transmembrane protease serine 15 {ECO:0000256|PIRNR:PIRNR001138};
GN   Name=TMPRSS15 {ECO:0000313|Ensembl:ENSPTRP00000023779,
GN   ECO:0000313|VGNC:VGNC:3728};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000023779, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000023779, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the
RT   human genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|Ensembl:ENSPTRP00000023779, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136134; DOI=10.1038/nature04101;
RA   Hughes J.F., Skaletsky H., Pyntikova T., Minx P.J., Graves T.,
RA   Rozen S., Wilson R.K., Page D.C.;
RT   "Conservation of Y-linked genes during human evolution revealed by
RT   comparative sequencing in chimpanzee.";
RL   Nature 437:100-103(2005).
RN   [3] {ECO:0000313|Ensembl:ENSPTRP00000023779}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
CC   -!- FUNCTION: Responsible for initiating activation of pancreatic
CC       proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase
CC       A). It catalyzes the conversion of trypsinogen to trypsin which in
CC       turn activates other proenzymes including chymotrypsinogen,
CC       procarboxypeptidases, and proelastases.
CC       {ECO:0000256|PIRNR:PIRNR001138}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Activation of trypsinogen by selective cleavage of 6-
CC         Lys-|-Ile-7 bond.; EC=3.4.21.9;
CC         Evidence={ECO:0000256|PIRNR:PIRNR001138};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|PIRNR:PIRNR001138};
CC       Single-pass type II membrane protein
CC       {ECO:0000256|PIRNR:PIRNR001138}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|PIRNR:PIRNR001138, ECO:0000256|SAAS:SAAS00559343}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR   EMBL; AACZ04064206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ04064207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ04064208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_514836.3; XM_514836.4.
DR   STRING; 9598.ENSPTRP00000023779; -.
DR   MEROPS; S01.156; -.
DR   PaxDb; H2QKV6; -.
DR   Ensembl; ENSPTRT00000025763; ENSPTRP00000023779; ENSPTRG00000013800.
DR   GeneID; 458478; -.
DR   KEGG; ptr:458478; -.
DR   CTD; 5651; -.
DR   VGNC; VGNC:3728; TMPRSS15.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00940000159353; -.
DR   InParanoid; H2QKV6; -.
DR   KO; K01316; -.
DR   OMA; HKSCGKK; -.
DR   OrthoDB; 1314811at2759; -.
DR   TreeFam; TF351678; -.
DR   Proteomes; UP000002277; Chromosome 21.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005044; F:scavenger receptor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd00041; CUB; 2.
DR   CDD; cd00112; LDLa; 2.
DR   CDD; cd06263; MAM; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.60.120.290; -; 2.
DR   Gene3D; 3.10.250.10; -; 1.
DR   Gene3D; 3.30.70.960; -; 1.
DR   Gene3D; 4.10.400.10; -; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR000998; MAM_dom.
DR   InterPro; IPR011163; Pept_S1A_enterop.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR000082; SEA_dom.
DR   InterPro; IPR036364; SEA_dom_sf.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR001190; SRCR.
DR   InterPro; IPR017448; SRCR-like_dom.
DR   InterPro; IPR036772; SRCR-like_dom_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF00057; Ldl_recept_a; 2.
DR   Pfam; PF00629; MAM; 1.
DR   Pfam; PF01390; SEA; 1.
DR   Pfam; PF15494; SRCR_2; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001138; Enteropeptidase; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00192; LDLa; 2.
DR   SMART; SM00137; MAM; 1.
DR   SMART; SM00200; SEA; 1.
DR   SMART; SM00202; SR; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF49854; SSF49854; 2.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF56487; SSF56487; 1.
DR   SUPFAM; SSF57424; SSF57424; 2.
DR   SUPFAM; SSF82671; SSF82671; 1.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS01209; LDLRA_1; 2.
DR   PROSITE; PS50068; LDLRA_2; 2.
DR   PROSITE; PS00740; MAM_1; 1.
DR   PROSITE; PS50060; MAM_2; 1.
DR   PROSITE; PS50024; SEA; 1.
DR   PROSITE; PS50287; SRCR_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002277};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00124,
KW   ECO:0000256|SAAS:SAAS00037407};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001138,
KW   ECO:0000256|RuleBase:RU363034};
KW   Membrane {ECO:0000256|PIRNR:PIRNR001138};
KW   Protease {ECO:0000256|PIRNR:PIRNR001138,
KW   ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW   Serine protease {ECO:0000256|PIRNR:PIRNR001138,
KW   ECO:0000256|RuleBase:RU363034}.
FT   DISULFID    643    655       {ECO:0000256|PROSITE-ProRule:PRU00124}.
FT   DISULFID    650    668       {ECO:0000256|PROSITE-ProRule:PRU00124}.
FT   DISULFID    662    677       {ECO:0000256|PROSITE-ProRule:PRU00124}.
FT   DISULFID    757    767       {ECO:0000256|PROSITE-ProRule:PRU00196}.
SQ   SEQUENCE   1019 AA;  113120 MW;  4A6202DCCEDD4335 CRC64;
     MGSKRSVSSR HHSLSSYEIM FAALFAILVV LCAGLIAVSC LTIKESQRGA TLGQSHEARG
     TFKITSGVTY NPNLQDKLSV DFKVLAFDLQ QMIDEIFLSS NLKNEYKNSR VLQFENGSII
     VIFDLFFAQW VSDENVKEEL IQGLEANKSS QLVTFHIDLN SVDILDKLTT TSHLATPGNV
     SIECLPGSSP CTDALTCIKA DLFCDGEVNC PDGSDEDNKM CATVCDGRFL LTGSSGSFQA
     THYPKPSETS VVCQWIIRVN QGLSIKLSFD DFNTYYTDIL DIYEGVGSSK ILRASIWETN
     PGTIRIFSNQ VTATFLIESD ESDYVGFNVT YTAFNSSELN NYEKINCNFE DGFCFWVQDL
     NDDNEWERIQ GSTFSPFTGP NFDHTFGNAS GFYISTPTGP GGRQERVGLL SLPLYPTLEP
     ACLSFWYHMY GENVHKLSIN ISNDQNMEKT VFQKEGNYGD NWNYGQVTLN ETVKFKVAFN
     AFKNKILSDI ALDDISLTYG ICNGSLYPEP TLVPTPPPEL PTDCGGPFEL WEPNTTFSSM
     NFPNSYPNLA FCVWILNAQK GKNIQLHFQE FDLENINDVV EIRDGEEADS LLLAVYTGPG
     PVKDVFSTTN RMTVLLITND VLARGGFKAN FTTGYHLGIP EPCKEDHFQC KNGECVPLVN
     LCDGHLHCED GSDEADCVRF FNGTMNNNGL VRFRIQSIWH TACAENWTIQ ISNDVCQLLG
     LGSGNSSVPI FSTDGGPFVK LNTAPDGHLI LTPSQQCLQD SLIRLQCNHK SCGKKLAAQD
     ITPKIVGGSN AKEGAWPWVV GLYYGGRLLC GASLVSSDWL VSAAHCVYGR NLEPSKWTAI
     LGLHMKSNLT SPQTVPRLID EIVINPHYNR RRKDNDIAMM HLEFKVNYTD YIQPICLPEE
     NQVFPPGRNC SIAGWGTVVY QGTTANILQE ADVPLLSNEK CQQQMPEYNI TENMICAGYE
     EGGIDSCQGD SGGPLMCQEN NRWFLAGVTS FGYKCALPNR PGVYARVSRF TEWIQSFLH
//
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