ID W5Q241_SHEEP Unreviewed; 1038 AA.
AC W5Q241;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 63.
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:ENSOARP00000016779.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000016779.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000016779.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000016779.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000016779.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Responsible for initiating activation of pancreatic
CC proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A).
CC It catalyzes the conversion of trypsinogen to trypsin which in turn
CC 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-Lys-|-
CC Ile-7 bond.; EC=3.4.21.9; Evidence={ECO:0000256|PIRNR:PIRNR001138};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606,
CC ECO:0000256|PIRNR:PIRNR001138}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606, ECO:0000256|PIRNR:PIRNR001138}.
CC -!- SIMILARITY: Belongs to the DMBT1 family.
CC {ECO:0000256|ARBA:ARBA00009931}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|PIRNR:PIRNR001138}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR EMBL; AMGL01006515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01006516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01006517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01006518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01006519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01006520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01006521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01006522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5Q241; -.
DR SMR; W5Q241; -.
DR STRING; 9940.ENSOARP00000016779; -.
DR PaxDb; 9940-ENSOARP00000016779; -.
DR Ensembl; ENSOART00000017017.1; ENSOARP00000016779.1; ENSOARG00000015635.1.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_011803_0_0_1; -.
DR OMA; THGICNG; -.
DR Proteomes; UP000002356; Chromosome 1.
DR Bgee; ENSOARG00000015635; Expressed in duodenum and 8 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00112; LDLa; 2.
DR CDD; cd06263; MAM; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR Gene3D; 3.30.70.960; SEA domain; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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; IPR043504; Peptidase_S1_PA_chymotrypsin.
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 PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF15; TRANSMEMBRANE SERINE PROTEASE 15; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF00629; MAM; 1.
DR Pfam; PF01390; SEA; 1.
DR Pfam; PF00530; SRCR; 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; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 2.
DR SUPFAM; SSF82671; SEA domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR SUPFAM; SSF56487; SRCR-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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; PS00420; SRCR_1; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001138};
KW Membrane {ECO:0000256|PIRNR:PIRNR001138, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR001138};
KW Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR001138};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..169
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 240..351
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 362..521
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 541..653
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 697..807
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 804..1038
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 844
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001138-1"
FT ACT_SITE 895
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001138-1"
FT ACT_SITE 990
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001138-1"
FT DISULFID 662..674
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 669..687
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 681..696
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 776..786
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 1038 AA; 115283 MW; 064DCD40CE6744F7 CRC64;
MGSKRSVPSR RHSLTTYEVM FAVLFVMLVA LCAGLIAVSW LSIQGSEKDA AFGKSHEARG
TLKIISGATY NSHLQDKLSV DFKVLAFDIQ QMIDDIFQSS NLKNEYKNSR VLRFENGSII
VIFDLLFVQW VSDKNVKEEL IQGIEANKSS QLVTFHIDLN SIDITAPLEN FSTISPATTS
EKLTTSIPLA TPGNVSIECP PDSRLCGDAL KCIAIDLFCD GELNCPDGSD EDNKTCATAC
DGRFLLTGSS GSFEALHYPK PSNNTSAVCR WIIRYVNQGL SIQLNFDYFN TYYADVLNIY
EGMGSSKILR ASLWSNNPGI IRIFSNQVTA TFLIQSDESD YIGFKVTYTT FNSKELNNYE
KINCNFEDGF CFWIQDLNDD NEWERTQGST FPPSTGPTFD HTFGNESGFY ISTPTGPGGR
RERVGLLTLP LDPTPEQACL SFWYYMYGEN VYKLSINISS DQNTEKTIFQ KEGNYGQNWN
YGQVTLNETV EFKVAFYGFK NQFLSDIALD DISLTYGICN VSVYPEPTLV PTLPPELPTD
CGGPHELWEP NTTFTSINFP NNYANQAFCV WNLNAQKGKN IQLHFQEFDL ENIADVVEIR
DGEGDDSLFL GAAVYTGPGP VKDVFSTTNQ MTVLFITDDM LVKRGFKANF TTGYGLGIPE
PCKEDNFQCK NGECIPLVNL CDGFPHCKDG SDEAPCVRLF NGTTDRSGLV QFRIQSIWHV
ACAENWTTQI SDDVCQLLGL GTGNSSMPTF STGGGPFVKL NTAPNGSLIL TPSQQCLEDS
LILLQCNYKS CGKKLVTREV SPKIVGGNDS REGAWPWVVA LYFNDQQVCG ASLVSRDWLV
SAAHCLYGRN LEPSKWKAVL GLYMASNPTS PQIETRLIDQ IVINPHYNKR RKDSDIAMMH
LELKVNYTDY IQPICLPGEN QVFSPGRICS IAGWGTLAYQ GSTADVLQEA DVPLLSNEKC
QQQMPEYNIT ENMVCAGYEA GGVDSCQGDS GGPLMCQENN RWLLAGVTSF GYQCALPNRP
GVYARVPRFT EWIQSFLH
//
