ID K7GET1_PELSI Unreviewed; 1027 AA.
AC K7GET1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Transmembrane serine protease 15 {ECO:0000313|Ensembl:ENSPSIP00000018792.1};
GN Name=TMPRSS15 {ECO:0000313|Ensembl:ENSPSIP00000018792.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000018792.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000018792.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AGCU01125543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01125544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01125545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K7GET1; -.
DR STRING; 13735.ENSPSIP00000018792; -.
DR Ensembl; ENSPSIT00000018878.1; ENSPSIP00000018792.1; ENSPSIG00000016555.1.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000159353; -.
DR HOGENOM; CLU_011803_0_0_1; -.
DR OMA; THGICNG; -.
DR TreeFam; TF351678; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
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:SF8; ACROSIN; 1.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 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 PRINTS; PR00020; MAMDOMAIN.
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; 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 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:UP000007267};
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 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..172
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 229..338
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 349..508
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 530..642
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 686..796
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 793..1027
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 651..663
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 658..676
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 670..685
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 765..775
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 1027 AA; 114406 MW; 16E8E5154D8E3D13 CRC64;
MNLKKSLSKR GIPLNDFEIW LAALLAIFVC VCAGLITLSW LLIKESQQAI PTEVNENSHA
ATGTFKILSG ASFSPSLEDN SSADFKALAF DIQQLITEIY QASQLKNEYK NSEVLLFKNG
SIIVVFRLNF AQWVSNEKAK NELVLGIEAN KTSLLKTINI DVNSIEVTDS EQLTTSNSST
TSVISVKCLP SEESCADAIN CISKNLYCDG LPNCPDGSDE IDSICATTCD GKFMLTGSSG
SFHSINYPKP YNSNIVCQWI IRTNHGLSIK LNFTSFDTQQ YTDILNIYEG TGPSKILRAS
LWGTNPGTVY IFSDEATAEF ITDYSENYNG FNATYTTFHT SELSNNEKIN CNFEDSFCYW
SQDLEDDGEW ERISGPTFPF MSGPDYDHTY GNLSGFYIST PIGFTTRQQR VRLFSLPLVP
ASDPFCLRFW YHMYGTNVYR FSIKITNSNN MEKTVFQREG NYGNNWNYGQ VTLNETSNFK
VIFDAFKNPG LSDIALDDIG LTSGKCKESI YPEPTVVPTT TTPSPLPTDC GGPFELWEPN
TTFSSKNYPN NYPDQASCIW YLNAEKGKNI QLHFQYFYLE DIYDVVEIRD GRGNNSLFLG
IAVYTGQNSV PDVYSTTNQM TVLFITDKSG TRKGFLANFT TGYNLGMPAP CGPKDYQCGS
GECIPLDNLC DGHLQCKDGS DETECVHLFN GSLSVNGLVQ FRIENKWYIA CADYWSEQIS
NDVCNALGLG NMNTSSTMST TGNGPFVKIT KAANQSTILM PSKQCLNNLV MYLQCNDKPC
GKQLITQQIN GKIVGGSDAK EGAWPWVVSL FFKDRPTCGA SLLSDEWLVS AAHCVYGRNL
IPSQWKAVLG LHTTLNLTYP QTVIQEIDQI VINPHYNKRT KNNDIAMMHL QFKVNYTDYI
QPICLPEASQ QFLPGINCFI AGWGRTVYQG STANILQEAE VPLITNEKCQ QQLPQYNITE
NMMCAGYDEG GVDSCQGDSG GALMIQDNSR WLLAGVTSFG YQCALPQRPG VYARVTQFVD
WIKQFIH
//
