ID M4A0S3_XIPMA Unreviewed; 811 AA.
AC M4A0S3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Transmembrane serine protease 6 {ECO:0000313|Ensembl:ENSXMAP00000008067.2};
GN Name=TMPRSS6 {ECO:0000313|Ensembl:ENSXMAP00000008067.2};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000008067.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000008067.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000008067.2};
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}.
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; M4A0S3; -.
DR STRING; 8083.ENSXMAP00000008067; -.
DR Ensembl; ENSXMAT00000008077.2; ENSXMAP00000008067.2; ENSXMAG00000008048.2.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000160104; -.
DR HOGENOM; CLU_006842_19_3_1; -.
DR InParanoid; M4A0S3; -.
DR OMA; WFALQIP; -.
DR Proteomes; UP000002852; 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; 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; 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; 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:UP000002852};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 45..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; 90062 MW; 34DC8D9CC9D4F282 CRC64;
MALGCGSKES LSCDREVTPA SLSNEVGAAT QNVELQIKTT RTCRFLLASL VVLIVFLIAV
AAALAWYFLE YSVWTLEPRV QHQYTAYLTI VNRNFSADLA CHSNPVFKTE AKYVENTLKK
ILKASSLSRY FNYTTVFAFG QGSVVAHFWI VLSVPSSHVG KVTVEEVTRS LEDGLRWYGR
SQRGETANVD GFLFHLPTLC VTETDSKVVE VLTSSFDCYR YQKVVSSSPV ALRGPETHRP
SCLWHLQTDP GSQLELHMEW LLPECRDRLV VYDSITPSDH HLITSVYGCS RHEDVVRVLS
SGEWMTVVWK KGLYNYKDPF SLSAQAWPQQ DCISSVQLKE VQGVQGILQT PFFPSFYPPN
TNCTWTFIMP GAALGLALEF EGYELSRASY NQACTQGQWV IQNRRLCGTR GLQPYCERLS
LLTHSTTVVM TSEVSLTGPG LQVHYSIFNL SDPCPGQFLC TVSGLCVPLC DGIKDCSNGL
DERNCVCVAQ YKCPEDSQCV DYYKVCDQHP DCPEASDEMN CTDGVECTDM TYVCADGTCL
KKPNPECDSV TDCPDASDEN RCECGLRQFS TRIVGGSDAS EGEWPWQTSL QVRGTHICGG
ALISSQWVAS AAHCFYDDSV YSPSVWTVYL GKLLLNRSSS IEEVARVQQI HLHQYYDSES
HDYDLALLKL DRPAYALLTG HARPACLPPA THQLEPGLLC WVTGWGAQQE GGRTNNVLQK
VDVRLVSEEA CVRSYGYLVT PRMLCAGYRS GGKDACQGDS GGPLVCQEPS GRWFLAGVVS
WGKGCGRPDY YGVYTRITRL TDWIKQVISS P
//