ID A0A493SWU5_ANAPP Unreviewed; 758 AA.
AC A0A493SWU5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Transmembrane serine protease 6 {ECO:0000313|Ensembl:ENSAPLP00000017973.1};
GN Name=TMPRSS6 {ECO:0000313|Ensembl:ENSAPLP00000017973.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000017973.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000017973.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000017973.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A493SWU5; -.
DR Ensembl; ENSAPLT00000040498.1; ENSAPLP00000017973.1; ENSAPLG00000000590.2.
DR GeneTree; ENSGT00940000160104; -.
DR Proteomes; UP000016666; Chromosome 1.
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; 3.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 3.
DR Gene3D; 3.30.70.960; SEA domain; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
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; IPR001314; Peptidase_S1A.
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; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF12; LOW QUALITY PROTEIN: TRANSMEMBRANE PROTEASE SERINE 6; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00057; Ldl_recept_a; 2.
DR Pfam; PF01390; SEA; 1.
DR Pfam; PF00089; Trypsin; 2.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00192; LDLa; 3.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 2.
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; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 3.
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:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW Serine protease {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 34..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..191
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 317..434
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 559..758
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 440..452
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 456..471
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 492..507
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 513..525
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 533..548
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 758 AA; 84818 MW; E169046B9FF5781C CRC64;
MPQMEAEEQE EDANSLSKDG SETNSTTSRD CRRYVPLGIV FVLLAGTAAT TWYFLDYRPW
HLEPSVLQFY SGSLQVLNRQ YFPDLGEVES RAFWLESAKL QNMLKDLIRA TELGRYYNSS
TVYAFGEGAL TFFFWFTLQI PESKQKEMTA ETVNTMLHQE LSASFNISGS LSYQAEYRVN
PDSLVLLESS VKDIVVLKST LGCYRYSYVQ EDDILTLEGP DYLASSCLWH LHGLKGYMIK
LHLEWTLPDC RDRLAMYDAA GPLEKHLITS IYGCSRQEPV VEVLSSGPVM SIVWKKAMYS
YYDPFILTAQ VVPLKACEVN ITLREGLELQ GKISTPHYPS YYSPNTQCTW HMMVPSLGYG
VTLWFDAYAL SRQKQDLPCT QGQWIIQNRR LCGLRTLQAY AERIPVTSSA DITITFTSQI
SLTGPGVQAA YSLYNLSDPC PGEFLCSVNG LCVPACDGIK DCPNGLDERN CVCPAKFQCR
EDSTCIEFSR VCNQQRDCAN GTDEEQCSEG VPCGPFTHRC DDGTCVKKPN PRCDTTADCR
DLSDEERCDC GLQAPLSRIV GGANSVEGEW PWQASLQVRG RHICGGTLIA DRWVVSAAHC
FQDERLASPS IWTVYLGKYF QNTSSHTEVS FKPICLPAPS HLFEPGLHCW ITGWGALKEG
GHISNVLQKV DVQIIQQDIC SEAYHYMISP RMLCAGYRKG KKDACQGDSG GPLACEEPSG
RWFLAGLVSW GMGCARPNSY GVYTRITQVL GWMNQTMS
//
