ID F6X0X4_XENTR Unreviewed; 806 AA.
AC F6X0X4;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Transmembrane protease serine 6 isoform X1 {ECO:0000313|RefSeq:XP_004913946.2};
DE SubName: Full=Transmembrane serine protease 6 {ECO:0000313|Ensembl:ENSXETP00000035000};
GN Name=tmprss6 {ECO:0000313|Ensembl:ENSXETP00000035000,
GN ECO:0000313|RefSeq:XP_004913946.2,
GN ECO:0000313|Xenbase:XB-GENE-1011573};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000035000};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000035000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000035000};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000035000}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2011) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_004913946.2}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_004913946.2};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_004913946.2};
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_004913946.2; XM_004913889.3.
DR Ensembl; ENSXETT00000035000; ENSXETP00000035000; ENSXETG00000016040.
DR AGR; Xenbase:XB-GENE-1011573; -.
DR Xenbase; XB-GENE-1011573; tmprss6.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_19_3_1; -.
DR OMA; WFALQIP; -.
DR TreeFam; TF330647; -.
DR Reactome; R-XTR-1442490; Collagen degradation.
DR Reactome; R-XTR-1474228; Degradation of the extracellular matrix.
DR Proteomes; UP000008143; Chromosome 4.
DR Bgee; ENSXETG00000016040; Expressed in liver.
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; 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; 2.
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; 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; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00192; LDLa; 3.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 3.
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; 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 ECO:0000313|RefSeq:XP_004913946.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008143};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|RefSeq:XP_004913946.2};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 42..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 75..194
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 325..441
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 571..806
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 447..459
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 463..478
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 499..514
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 525..537
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 545..560
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 806 AA; 89436 MW; 571075FB24C6F805 CRC64;
MSLHLPLPDT LTAPMEKDPK DLSQDSVCVG MPEKPKWTSR DWLRFAPLWM VLVLIAGAGL
TWYILEVDTS PVLRISKLYS CSLNIVSHEL TYDLTRPESS SFRTEAAHLQ KLVNGLVLAS
ELAAYHNSCT VYAFGEGSLK IYFWVSLEVP NTDLKYVTES SVTAALNSVL HKKTNSKGHY
IFDQYHVDPN SLDILEASVH DIQLLSSSAG CYRYSYVRAG QEIRLKGPDY LSPSCVWHLQ
GPPAYLIRLR LKWTRSECRD RLAMYDAAAP LETHLITSHY GCSRQEPISE ILSSGSTMLV
VWKQAMYSYY DPFVLTVLPL PVESCQHTIE MTEGLEIQGH LRTPYYPRYY PPKPQCTWNI
TVPSPEYGVV LWFEGYMLTR RYTYAPCMQG QWQIQNRRMC GVRVLQSYAE RIDPVSGNVT
VSFTCPASLT GPGVQASYSL YNQSDPCPGE FLCAVNGLCV PLCDGVKDCP NELDERNCVC
PAQYHCPGAE SCISITSVCD GKKDCANGTD EELCNQGANF PTAACGAFNY KCADGSCVQK
PNAECDSIAD CPDGSDENNC GCGIQAVGIR LVGGTQAQEG EWPWQASLQV RGEHICGGTL
VADQWILTAA HCFTPESYAS PEVWTVYLGK VRLSRSTQKE LAFKVIRLVI HPFYDEDSHD
YDVALVLLDH LVPLTSPHVQ PICLPSSTHH FPTGSSCWVT GWGSVKENGP TSDVLQKVDI
QLVAQDICTE LYRYQISPRM LCAGYRDGSK DACQGDSGSP LVCKTASGRW FQAGLVSWGA
GCGIPRYFGV YSRITRLVQW IESITL
//
