ID A0A2K5P1B2_CERAT Unreviewed; 1019 AA.
AC A0A2K5P1B2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Transmembrane serine protease 15 {ECO:0000313|Ensembl:ENSCATP00000043455.1};
GN Name=TMPRSS15 {ECO:0000313|Ensembl:ENSCATP00000043455.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000043455.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000043455.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the DMBT1 family.
CC {ECO:0000256|ARBA:ARBA00009931}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR RefSeq; XP_011885212.1; XM_012029822.1.
DR AlphaFoldDB; A0A2K5P1B2; -.
DR STRING; 9531.ENSCATP00000043455; -.
DR Ensembl; ENSCATT00000067894.1; ENSCATP00000043455.1; ENSCATG00000044263.1.
DR GeneID; 105571817; -.
DR KEGG; caty:105571817; -.
DR CTD; 5651; -.
DR GeneTree; ENSGT00940000159353; -.
DR OMA; THGICNG; -.
DR OrthoDB; 4252799at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00112; LDLa; 2.
DR CDD; cd06263; MAM; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.60.120.200; -; 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; 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; 2.
DR Pfam; PF00629; MAM; 1.
DR Pfam; PF01390; SEA; 1.
DR Pfam; PF15494; SRCR_2; 1.
DR Pfam; PF00089; Trypsin; 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|RuleBase:RU363034};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034};
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 225..334
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 345..504
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 524..634
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 678..788
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 785..1019
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 643..655
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 650..668
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 662..677
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 757..767
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 1019 AA; 112906 MW; FCA319A013481181 CRC64;
MGSKRSVSSR HHSLSSYEIM FATLFAILVV LCAGLIAVSW LTIKESQRGA ALGQSHEVRG
TFKITSGVTY NPNLQDKLSV DFKVLAFDLQ QMIDEIFLSS NLKNEYKNSR VLQFENGSII
VTFELFFAQW VSDENVKEEL IQGVEANKSS QLVTFHIDLN SVDILGKLTT TSHLATPGNV
SVECPPGSSP CADALTCIKA DLFCDGEVNC PDGSDEDNKM CATVCDGRFL LTGSSGSFQA
THYPKPSESG VVCQWIIRVN QGLSIKLSFD HFNIYYTDTL NIYEGVGSSK ILRASIWETN
PGTMRIFSNQ VTATFLIESD ESDYVGFNVT YTAFNSSELN NYEKINCNFE DGFCFWVQDL
NDDNEWERIQ GSTFPPFTGP NFDHTFGNAS GFYISTPTGP GGRKEHVGLL SLPLDPTLEP
VCLSFWYHMY GENVHKLSIN ISNDQNMEKT VFQKEGNYGE NWNYGQVTLN ETVKFKVGFH
AFKNKILSDI ALDDISLTHG ICNGSLYPEP TLVPTPPPEL PTDCGGPFEL WEPNTTFSSM
NFPNSYPNLA FCVWILNAQK GKNIQLHFQE FDLENINDVV EIRDGGEADS LFLTVYTGPG
PVKDVFSTTN RMTVLLITND ALARGGFKAN FTTGYHLGIP EPCKEDNFQC KNGECVPLAN
LCDGHLHCED GSDEADCVRL FNGTTNNNGL VQFRIQSLWH TACAENWTTH ISNDVCQLLG
LGSGNSSMPI FSTNGGPFVK LNTAPDGSLI LTPSQQCLQD SLIRLRCNHK SCGKKLVAQD
ITPKIVGGSN AEEGAWPWVV GLYYGGRLLC GASLVSSDWL VSAAHCVYGR NLEPSKWTAV
LGLHMTSNLN SPQTVSRLID QIVINPHYNR RRKDNDIAMM HLEFKVNYTD YIQPICLPEE
NQVFPAGRNC SIAGWGRVVY QGSTANILQE ADVPLLSNEK CQQQMPEYNI TENMICAGYE
EGGIDSCQGD SGGPLMCQEN NRWFLAGVTS FGYKCALPNR PGVYARVPRF TEWIQSFLH
//
