ID A0A3Q0DCB7_MESAU Unreviewed; 1099 AA.
AC A0A3Q0DCB7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Transmembrane protease serine 9 {ECO:0000313|RefSeq:XP_021090458.1};
GN Name=Tmprss9 {ECO:0000313|RefSeq:XP_021090458.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021090458.1};
RN [1] {ECO:0000313|RefSeq:XP_021090458.1}
RP IDENTIFICATION.
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}.
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DR RefSeq; XP_021090458.1; XM_021234799.1.
DR AlphaFoldDB; A0A3Q0DCB7; -.
DR STRING; 10036.ENSMAUP00000006366; -.
DR Proteomes; UP000189706; 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; cd00112; LDLa; 1.
DR CDD; cd00190; Tryp_SPc; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 3.30.70.960; SEA domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 3.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
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; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF13; TRANSMEMBRANE SERINE PROTEASE 12; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF01390; SEA; 1.
DR Pfam; PF00089; Trypsin; 3.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00020; Tryp_SPc; 3.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF82671; SEA domain; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 3.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50024; SEA; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 3.
DR PROSITE; PS00134; TRYPSIN_HIS; 2.
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:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU363034,
KW ECO:0000313|RefSeq:XP_021090458.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|RefSeq:XP_021090458.1};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 55..173
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 239..485
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 546..779
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 868..1098
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 423..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 190..202
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 210..225
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1099 AA; 118361 MW; 96F7A8D90C98C1EC CRC64;
MERTAPDLQL MPEMTKDTHV PAPDSGCCRT AVTAVVAVST VVLTLGVLLA FLSAQGVLVE
HTAQLQGIRF SSSLQQETSH YYRLLTPALQ TLFVSSFHKT QLESSCAGCT VLSYRDGNSS
VFVHFRLHFL LRALQPLSLD QEEDILQKGI QARLQGHGLS LAAYGTIVSV RLTGRCDSPV
TERDLKSGRC PGNAFSCDNS QCVNKENPEC DTRVDCSDGS DEAQCDCGWQ PAWRSAGRIV
GGVEAAPGEF PWQVSLRENH EHFCGATIIG DRWLVSAAHC FNEFQDPAQW AAQAGSVLLS
GSEASAVRAR VLRIAKHPAY DADTADFDVA VLELARPLPF GRYVQPACLP AATHVFPPRK
KCLISGWGYL KEDFLVKPEV LQKATVELLE QSLCARLYGH ALTDRMLCAG YLDGKVDSCQ
VRRQPRPLPR GRANRRGVRG RAPAAPGGVG AARAAWGRLT PCRSVCVRLG SVHAGAAVWV
LPCLLGFRDR ASPVARGGLE LRTRPPALPG AGHPSAGLAV TAGACREHLH VTECGARPAM
DKPTRIVGGL SAVSGEVPWQ ASLKEGSRHF CGATVVGDRW LLSAAHCFNH TKTAEQVQAH
LGTVSLMGVG GSPVKLGLRR VFLHPQYNPG ILDFDMALLE LARPLVFNKY IQPICLPLAI
HKFPVGRKCM ISGWGNTQEG NATKPDILQK ASVGIIEQKM CGSLYNFSLT DRMLCAGFLE
GRVDSCQGDS GGPLACEETP GVFYLAGIVS WGIGCAQAKR PGVYARITRL KDWILRVMSS
GLNSTPHPHT SSTQLIPNQP ARTTEATTSR PATPRGTSRV TTKPPNTTLA AWSTTTRGQT
PAANAPGAAT HSQLPDCGLA PPGALTRIVG GSSASRGEWP WQVSLWLQHR EHRCGAVLVA
DRWLLSAAHC FDTYGDPVQW AAFLGTPFLS GAEGQLKRVV RIYRHPFYNL YTLDYDVALL
ELAGPVHRSR LVRPICLPGP ARPPEGARCV ITGWGSLREG GSMAVQLQKA AVRVLSEQAC
RRFYPVQISS RMLCAGFPQG GVDSCSGDAG GPLACREPSG QWVLTGVTSW GYGCGRPHFP
GVYTRVAAVL GWITQSIQE
//
