ID A0A087XG16_POEFO Unreviewed; 811 AA.
AC A0A087XG16;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Transmembrane serine protease 6 {ECO:0000313|Ensembl:ENSPFOP00000004719.2};
GN Name=TMPRSS6 {ECO:0000313|Ensembl:ENSPFOP00000004719.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000004719.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000004719.2}
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 EMBL; AYCK01018856; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007578045.1; XM_007577983.2.
DR AlphaFoldDB; A0A087XG16; -.
DR STRING; 48698.ENSPFOP00000004719; -.
DR MEROPS; S01.308; -.
DR Ensembl; ENSPFOT00000004728.2; ENSPFOP00000004719.2; ENSPFOG00000004655.2.
DR GeneID; 103156072; -.
DR KEGG; pfor:103156072; -.
DR CTD; 164656; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000160104; -.
DR OMA; WFALQIP; -.
DR OrthoDB; 4629979at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:InterPro.
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; 2.
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; 1.
DR InterPro; IPR000859; CUB_dom.
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; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
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; PF01390; SEA; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00042; CUB; 2.
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; PS50068; LDLRA_2; 3.
DR PROSITE; PS50024; SEA; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 46..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..194
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 332..448
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 573..809
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 454..466
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 470..485
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 506..521
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 527..539
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 547..562
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 811 AA; 90071 MW; 3A4B92421296C433 CRC64;
MALGCGSKES VSCDQEVTPA TLSNEVGAAT QNEELHIKTT RTSKCLLASL VFLFVFLIAV
AATLAWYFLE YSVWTLEPRV QQQYTAYLTI VNRNFSADLA SHNNPTFKTE AKYVQNTLKK
IMKASSLSRY FNYTTVFAFG QGSVVAHFWI VLSVPSSHVG KVTVKEVARS LEDGLRWYGR
SQRGETANVN GFLFHLPTLC VTETDSKVVE VLTSSFDCYR YQKVVSSSPM ALRGPETHRL
SCLWHLQTDP GSQLELHMEW LLPECRDRLV VYDSITPSDH HLITSMYGCS RHEDVVRVLS
SSEWMTVVWK KGLYNYKDPF SLSAQAWPQQ DCISSIQLKE VQGVQGTLQT PFFPSFYPPN
TNCTWTFIMP GAALGLALEF EGYELSRASY NEACTQGQWV IQNRRLCGTR GLQPYCERLS
LLTNSTTVVM TSEVSLTGPG LQVHYSVFNL SDPCPGQFLC TVSGLCVPLC DGIKDCSNGL
DERNCVCVAQ YMCPEDSQCV DYYKVCDQHP DCPEASDEMN CTAGVECTDM TYVCADGTCL
KKPNPECDSV TDCPDASDEN RCECGLRQFS TRIVGGSDAL EGEWPWQTSL QVRGTHICGG
ALISSQWVAS AAHCFYDDSV YSPSVWTVYL GKLLLNRSSS IEEVARVQQI HLHQYYDSES
HDYDLALLKL DRPAYALLTG HARPACLPPP THQLEPGLLC WVTGWGAQRE GGGANNVLQK
VDVRLVSEEA CVRSYGYLVT PRMLCAGYRS GGKDACQGDS GGPLVCQEPS GRWFLAGVVS
WGKGCGRPDY YGVYTRITRL TNWIKQVISS P
//
