TMPS7_RAT
ID TMPS7_RAT Reviewed; 833 AA.
AC P86091;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Transmembrane protease serine 7;
DE EC=3.4.21.-;
DE AltName: Full=Matriptase-3 {ECO:0000250|UniProtKB:Q8BIK6};
GN Name=Tmprss7 {ECO:0000312|RGD:1304655};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15057822};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
CC -!- FUNCTION: Serine protease which preferentially hydrolyzes peptides with
CC Arg at the P1 position. {ECO:0000250|UniProtKB:Q8BIK6}.
CC -!- SUBUNIT: Forms a heterodimer with SERPINA5. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BIK6};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8BIK6}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8BIK6}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AABR03078747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03079133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P86091; -.
DR SMR; P86091; -.
DR STRING; 10116.ENSRNOP00000041453; -.
DR GlyGen; P86091; 3 sites.
DR PaxDb; P86091; -.
DR UCSC; RGD:1304655; rat.
DR RGD; 1304655; Tmprss7.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; P86091; -.
DR PhylomeDB; P86091; -.
DR TreeFam; TF330647; -.
DR PRO; PR:P86091; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00112; LDLa; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.60.120.290; -; 2.
DR Gene3D; 3.30.70.960; -; 1.
DR Gene3D; 4.10.400.10; -; 3.
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 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; SSF49854; SSF49854; 2.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57424; SSF57424; 2.
DR SUPFAM; SSF82671; SSF82671; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 2.
DR PROSITE; PS50024; SEA; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Repeat; Serine protease; Signal-anchor; Transmembrane;
KW Transmembrane helix; Zymogen.
FT CHAIN 1..833
FT /note="Transmembrane protease serine 7"
FT /id="PRO_0000356158"
FT TOPO_DOM 1..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..829
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 92..220
FT /note="SEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 233..350
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 355..471
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 473..509
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 548..585
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 596..830
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 30..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 636
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 684
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 780
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT SITE 255..256
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 233..259
FT /evidence="ECO:0000255"
FT DISULFID 285..312
FT /evidence="ECO:0000255"
FT DISULFID 355..386
FT /evidence="ECO:0000255"
FT DISULFID 474..486
FT /evidence="ECO:0000255"
FT DISULFID 481..499
FT /evidence="ECO:0000255"
FT DISULFID 493..508
FT /evidence="ECO:0000255"
FT DISULFID 549..561
FT /evidence="ECO:0000255"
FT DISULFID 556..575
FT /evidence="ECO:0000255"
FT DISULFID 569..584
FT /evidence="ECO:0000255"
FT DISULFID 621..637
FT /evidence="ECO:0000255"
FT DISULFID 720..786
FT /evidence="ECO:0000255"
FT DISULFID 752..765
FT /evidence="ECO:0000255"
FT DISULFID 776..806
FT /evidence="ECO:0000255"
SQ SEQUENCE 833 AA; 93286 MW; 6EEABC2D008263D1 CRC64;
MDKEKSDPSC KSSDLKISNI SIQVVSVPGK LPGRRLPRKP IGKARPRKQP KKRAPFWNVQ
NKIILFTVFL FILAVTAWTL LWLYISKTDS KDAFYFVGMF RITNIEFLPE YRQKESREFL
SMAKTVQQVV NLVYTTSAFS KFYKQSVVAD VSSNNKGGLL VHFWIVFVMP HAKGHIFCEE
CVAAILKDSI QTSITNRTSV GTLQGLAVDM DSVVLNAGLR SDYSSAVGSD NGCSQYFYAD
HLTLRYPLEI SATSGQLMCH FKLVAIVGYL IRLSIESIQL EADNCITDSL TVYDSLLPIR
ITCVLLSGYR ICEPTRTLMS FVSTNNLMLV TLKSPYVRRL AGIRAYFEVI PEQKCENTIL
VKEINSFEGK ISSPYYPSYY PPKCKCNWTF QTSLSTLGIA LKFHNYSITK KSMKGCEHGW
WEINEHMYCG SYMDHETIFR VPSPLVHIQL QCSSRLSDKP LLVEYGSYNI SQPCPAGSFR
CSSGLCVPQA QRCDGVNDCF DESDELFCVT AKPACNTSIF RQHGPLVCDG FQDCEDGQDE
QNCTRSIPCT NRTFKCGNDI CFRKQNAQCD GIVDCPDRSD EEGCGCSRSS PFLHRVVGGS
DSQEGTWPWQ VSLHFVGSAH CGASVISREW LLSAAHCFHG NRLSDPTPWT AHLGMYVQGN
AKFVSPVRRI VVHEYYNSQT FDYDIALLQL SIAWPETLRQ LIQPICIPPV GQRVRSGEKC
WVTGWGRRHE ADSKGSPILQ QAEVELIDQT VCVSTYGIIT SRMLCAGVMS GKSDACKGDS
GGPLSCRRKS DGKWILTGIV SWGYGCGRPN FPGVYTRVSN FVPWIHKYVP SLL
