ID I3MSS8_ICTTR Unreviewed; 358 AA.
AC I3MSS8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Transmembrane serine protease 11A {ECO:0000313|Ensembl:ENSSTOP00000015173.2};
GN Name=TMPRSS11A {ECO:0000313|Ensembl:ENSSTOP00000015173.2};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000015173.2, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000015173.2}
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}.
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DR EMBL; AGTP01067178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01067179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3MSS8; -.
DR STRING; 43179.ENSSTOP00000015173; -.
DR Ensembl; ENSSTOT00000025729.2; ENSSTOP00000015173.2; ENSSTOG00000025512.2.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000161698; -.
DR HOGENOM; CLU_006842_19_0_1; -.
DR InParanoid; I3MSS8; -.
DR TreeFam; TF351684; -.
DR Proteomes; UP000005215; 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; cd00190; Tryp_SPc; 1.
DR Gene3D; 3.30.70.960; SEA domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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; PF01390; SEA; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF82671; SEA domain; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
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};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 1..117
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 127..357
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 358 AA; 40674 MW; A6E3089647795653 CRC64;
MEYYHGTFKI SDLQVNSNSG QKSTYQLERL REMSEILVDE IFINSALNKH YIKNQIIRLT
PEIDGVKADI VMVFQFPSTE QRTVREKKIH SILNQKIRNE RALPIDVSSV QVNGCGKRAV
PLIVNRIMSG ELADKGAWPW QASLQRSNIH QCGATLISDR WLVTAAHCFK NNANPRQWTV
TFGTTINPPL MKREVKRIIV HERYHSPARE YDIAVVQFHP RVTFSDDIRR ICLPEASASF
PPNSTVYITG FGALYYGGES QNNLREAKVK IISNDVCKQP QVYGNDIKFG MFCAGYLEGI
YDACRGDSGG PLVIKDLKDT WYLIGIVSWG DNCGQKNKPG VYTQVTYYRR WIASKTGL
//
