ID A0A384DCS7_URSMA Unreviewed; 717 AA.
AC A0A384DCS7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Transmembrane protease serine 7 isoform X2 {ECO:0000313|RefSeq:XP_008704818.1};
GN Name=TMPRSS7 {ECO:0000313|RefSeq:XP_008704818.1};
OS Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_008704818.1};
RN [1] {ECO:0000313|RefSeq:XP_008704818.1}
RP IDENTIFICATION.
RC TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008704818.1};
RG RefSeq;
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_008704818.1; XM_008706596.1.
DR AlphaFoldDB; A0A384DCS7; -.
DR STRING; 29073.ENSUMAP00000005962; -.
DR GeneID; 103677322; -.
DR KEGG; umr:103677322; -.
DR CTD; 344805; -.
DR OrthoDB; 4629979at2759; -.
DR Proteomes; UP000261680; Unplaced.
DR GO; GO:0005886; C:plasma 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; 1.
DR CDD; cd00112; LDLa; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 4.10.1220.10; EGF-type module; 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; 2.40.10.10; Trypsin-like serine proteases; 2.
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; 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; 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; 1.
DR Pfam; PF00057; Ldl_recept_a; 2.
DR Pfam; PF01390; SEA; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00192; LDLa; 3.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 3.
DR SUPFAM; SSF82671; SEA domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 2.
DR PROSITE; PS50024; SEA; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Membrane {ECO:0000313|RefSeq:XP_008704818.1};
KW Protease {ECO:0000256|RuleBase:RU363034,
KW ECO:0000313|RefSeq:XP_008704818.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000261680};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000313|RefSeq:XP_008704818.1}.
FT DOMAIN 1..121
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 121..234
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 239..316
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 480..714
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 358..370
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 365..383
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 377..392
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 433..445
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 453..468
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 717 AA; 80057 MW; B74B8FB064617436 CRC64;
MFRITNIEFL PEYRQKESRE FLSVAWTVQQ VVNLIYTTSA FSEFYKQSVV ADVSNNKGGL
LVHFWIVFVM PHAKGHIFCE DCVAAILKDS IQTSIINRTS VGSLQGLAVD MDSVVLNDKG
CSQHLYADRL SLRYPLEISA TSGLLLCHFK LVAIVGYLIR LSIESVQIEA DNCVTDSLTI
YDSLLPIRSA ILYRICEPTR TVMSFVSTNN LMLVSFKSPH IRRLSGIRAF FEVIPEEKCE
NTVLVKEITG FEGKISSPYY PSYYPPKCKC TWKFQTSLST LGVALKFHNY SITKKSVKGC
DHGWWEINEH MYCGFYVDHQ TIFRVPSPLA HIQLRCGSRL SDKPLLVEYG SYNISQPCPA
GSFRCSSGLC VPQAQRCDGV NDCFDESDEL FCVTLKPACN ASSFRQHGRL VCDGFRDCED
GQDEQNCTQS IPCNDRTFKC GNDICFRKQN AQCDGTVDCP DGSDEEGCSC SRGSSTLHRI
IGGTDTQEGG WPWQVSLHFV GSAYCAASVI SSEWLLSAAH CFHGNRLSDP TPWTAHLGMY
VQGNAKFISP VKRIVVHEYY NSQTFDYDIA LLELSTAWPE TLKQLIQPIC IPPAGQKVRS
GEKCWVTGWG RRHEADNKGS PVLQQAEVEL IDQTLCVSTY GIITSRMLCA GVMSGKRDAC
RGDSGGPLSC RRKSDGKWIL TGIVSWGYGC GRPNFPGVYT RVSNFVPWIH KYVPSLL
//
