ID A0A8C3QMC8_9PASS Unreviewed; 1025 AA.
AC A0A8C3QMC8;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE SubName: Full=Transmembrane serine protease 15 {ECO:0000313|Ensembl:ENSCRFP00000008320.1};
OS Cyanoderma ruficeps (rufous-capped babbler).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Sylvioidea; Timaliidae; Cyanoderma.
OX NCBI_TaxID=181631 {ECO:0000313|Ensembl:ENSCRFP00000008320.1, ECO:0000313|Proteomes:UP000694396};
RN [1] {ECO:0000313|Ensembl:ENSCRFP00000008320.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCRFP00000008320.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000256|ARBA:ARBA00004398}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {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 AlphaFoldDB; A0A8C3QMC8; -.
DR Ensembl; ENSCRFT00000008616.1; ENSCRFP00000008320.1; ENSCRFG00000006520.1.
DR Proteomes; UP000694396; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0009566; P:fertilization; IEA:UniProtKB-ARBA.
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 FunFam; 2.60.120.290:FF:000043; Enteropeptidase; 1.
DR FunFam; 3.10.250.10:FF:000029; Enteropeptidase; 1.
DR FunFam; 2.60.120.200:FF:000128; enteropeptidase isoform X2; 1.
DR FunFam; 2.60.120.290:FF:000005; Procollagen C-endopeptidase enhancer 1; 1.
DR FunFam; 2.40.10.10:FF:000003; Transmembrane serine protease 3; 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; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF16; 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; PR00261; LDLRECEPTOR.
DR PRINTS; PR00020; MAMDOMAIN.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00192; LDLa; 2.
DR SMART; SM00137; MAM; 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; 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.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000694396};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..180
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 263..372
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 383..541
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 563..673
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 714..824
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 820..1025
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 179..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..209
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 679..691
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 686..704
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 698..713
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 793..803
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 1025 AA; 113815 MW; 02BA6B3D68C344CF CRC64;
MELKKTSDKK YVPLSSYEIF FASLLAIFVC VCVGLIVLSW LSIQELERAQ ADVNTHGYMG
IFKIVSGTSF TPTLQNSSSA DFKVLAFDVE KLIQNIFQES DLKYKFERCE ISWFKKSEDD
GDRLMSDTGV VVIFTLYFTQ MVPVVKVENE LILGVLANNP NPTKTLKIDV NSIQITGADE
NPTTMMPLTS SDPTSLTTSS LTPTSGSGLL TTSKSSTAVA ECLPPAELCA DGVTCISKDF
FCDGVLDCPD GSDESEKRCA AICDGKFMLT GSSGFFHSMN YPEPYNEDIV CQWIIVVPQG
LSIKLNFTSF ETQPYADILS IFEGLGQNKV LRASLSGTNF ETIYIFSHEA TAQFMSDYSE
NYNGFNATYT AFNASELNNY EKINCTFEDG FCFWIQDLED DSDWDRVQGP TFPLMSGPEF
DHTFGNLSGF YISTPIGLGF IEERVRILSL PLVPSDTYCL SFWYFMYAAN VYRLSISISD
ERGQEKIVFE KEGNYGNNWN YGQVTLNETS DFKVIFDAFK RRGASDIAVD DIGLTKGKCN
EDNYVEPTVR PTVPTTPLVP TDCGGPFELW EPNNTFSSAN FPNNYPNLAS CVWYLNAENG
KNIQLHFEVF DLESIHDVVE VRDGRGPDSL LLALYTEKGP LPDVFSTTNQ MTVILRTDKS
TTRKGFLANF TTGYHLRACT TDEHQCGSGK CIPLHNLCDN VPQCEDSSDE AKCMRLLNGS
LSTKGLVQAR IGKTWHLACA DDWSGEISDS VCQLLGLGDT NTSSAVLFTG DGPFVTITKG
GNHSLIFTKR EHCLDNLVIH LQCNIQSCGK HLATQNNGRI VGGSDARRGA WPWIVSLHFN
LQPVCGASLV SDEWLVTAAH CVYGRQLKPS RWKAALGLHL QSDLEKPPAV VHNIDRIIIN
PHYMKETKDS DIALMHLQHK VQYTDYIQPI CLPEKDQQFL PGINCSIAGW GNIEDEGPTS
NVLQEAEVPL LSNEKCQQWL PKYNITENML CAGYDMGGVD SCQQYGVCGT ETGWLSSRLM
RSTLT
//
