TMPS7_MOUSE
ID TMPS7_MOUSE Reviewed; 829 AA.
AC Q8BIK6; E9QME7; Q4PPC3;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Transmembrane protease serine 7;
DE EC=3.4.21.-;
DE AltName: Full=Matriptase-3;
GN Name=Tmprss7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RC STRAIN=C57BL/6 x NIH Black Swiss;
RX PubMed=15853774; DOI=10.1042/bj20050299;
RA Szabo R., Netzel-Arnett S., Hobson J.P., Antalis T.M., Bugge T.H.;
RT "Matriptase-3 is a novel phylogenetically preserved membrane-anchored
RT serine protease with broad serpin reactivity.";
RL Biochem. J. 390:231-242(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-829.
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Serine protease which preferentially hydrolyzes peptides with
CC Arg at the P1 position. {ECO:0000269|PubMed:15853774}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=240 nM for Suc-Ala-Ala-Pro-Arg-pNA {ECO:0000269|PubMed:15853774};
CC KM=534 nM for Suc-Ala-Ala-Pro-Lys-pNA {ECO:0000269|PubMed:15853774};
CC -!- SUBUNIT: Forms a heterodimer with SERPINA5. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15853774};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:15853774}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, eye, testis, skin, epididymis
CC and salivary gland with lower levels in heart, skeletal muscle, thymus,
CC ovary, prostate and uterus. {ECO:0000269|PubMed:15853774}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15853774}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC32448.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC32448.1; Type=Miscellaneous discrepancy; Note=Differs at the N-terminus for unknown reasons.; Evidence={ECO:0000305};
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DR EMBL; DQ061860; AAY66996.1; -; mRNA.
DR EMBL; AC166572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK045663; BAC32448.1; ALT_SEQ; mRNA.
DR CCDS; CCDS37347.2; -.
DR RefSeq; NP_766043.3; NM_172455.3.
DR RefSeq; XP_006521977.1; XM_006521914.2.
DR RefSeq; XP_006521978.1; XM_006521915.2.
DR AlphaFoldDB; Q8BIK6; -.
DR SMR; Q8BIK6; -.
DR BioGRID; 228959; 5.
DR STRING; 10090.ENSMUSP00000110209; -.
DR MEROPS; S01.072; -.
DR GlyGen; Q8BIK6; 2 sites.
DR PhosphoSitePlus; Q8BIK6; -.
DR PaxDb; Q8BIK6; -.
DR PRIDE; Q8BIK6; -.
DR Antibodypedia; 52124; 119 antibodies from 17 providers.
DR DNASU; 208171; -.
DR Ensembl; ENSMUST00000114562; ENSMUSP00000110209; ENSMUSG00000033177.
DR GeneID; 208171; -.
DR KEGG; mmu:208171; -.
DR UCSC; uc007ziu.1; mouse.
DR CTD; 344805; -.
DR MGI; MGI:2686594; Tmprss7.
DR VEuPathDB; HostDB:ENSMUSG00000033177; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000160085; -.
DR HOGENOM; CLU_006842_19_3_1; -.
DR InParanoid; Q8BIK6; -.
DR OMA; KPACNTS; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q8BIK6; -.
DR TreeFam; TF330647; -.
DR BioGRID-ORCS; 208171; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q8BIK6; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8BIK6; protein.
DR Bgee; ENSMUSG00000033177; Expressed in cerebellar cortex and 29 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
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; SM00042; CUB; 1.
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; 3.
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 1: Evidence at protein level;
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..829
FT /note="Transmembrane protease serine 7"
FT /id="PRO_0000027860"
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..346
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 351..467
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 469..505
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 503..540
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 544..581
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 592..826
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 26..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..52
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 632
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 680
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 776
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 255..256
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 233..259
FT /evidence="ECO:0000250"
FT DISULFID 285..308
FT /evidence="ECO:0000250"
FT DISULFID 351..382
FT /evidence="ECO:0000250"
FT DISULFID 470..482
FT /evidence="ECO:0000250"
FT DISULFID 477..495
FT /evidence="ECO:0000250"
FT DISULFID 489..504
FT /evidence="ECO:0000250"
FT DISULFID 511..530
FT /evidence="ECO:0000250"
FT DISULFID 524..539
FT /evidence="ECO:0000250"
FT DISULFID 545..557
FT /evidence="ECO:0000250"
FT DISULFID 552..571
FT /evidence="ECO:0000250"
FT DISULFID 565..580
FT /evidence="ECO:0000250"
FT DISULFID 617..633
FT /evidence="ECO:0000250"
FT DISULFID 716..782
FT /evidence="ECO:0000250"
FT DISULFID 748..761
FT /evidence="ECO:0000250"
FT DISULFID 772..802
FT /evidence="ECO:0000250"
FT CONFLICT 232
FT /note="G -> S (in Ref. 1; AAY66996)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="I -> T (in Ref. 1; AAY66996)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="P -> Q (in Ref. 3; BAC32448)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="V -> I (in Ref. 1; AAY66996)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="S -> I (in Ref. 1; AAY66996)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 829 AA; 92590 MW; 9B5971331CB23B6C CRC64;
MDKEKSDPSC KSSDLKISNI SIQVVSVPGK LPGRRPPRKP IGKPRPRKQP KKRAPFWNVQ
NKIILFTVFL FILAVTAWTL LWLYISKTES KDAFYFVGMF RITNIEFLPE YRQKESREFL
SMAKTVQQVV NLVYTTSAFS KFYKQSVVAD VSSNNKGGLL VHFWIVFVMP HAKGHIFCEE
CVAAILKDSI QTSIINRTSV GSLQGLAVDM DSVVLNAGLR SDYSSAVGSD NGCSRYLYAD
HLTLRYPLEI SATSGQLMCH FKLVAIVGYL IRLSIESIQL EADNCITDSL TVYDSLLPIR
SAILYRICEP TRTLMSFVST NNLMLVILKS PYVRRLAGIR AYFEVIPEQK CESTILVKEI
NSFEGKISSP YYPSYYPPKC KCTWTFQTSL STLGIALKFY NYSITKKSAK GCEHGWWEIN
EHMYCGSYMD HETIFRVPSP LVHIQLQCSS RLSDKPLLVE YGGYNISQPC PAGSFRCSSG
LCVPQAQRCD GVNDCFDESD ELFCVTVKPA CNSSSFRQHG PLVCDGFRDC EDGQDEQNCT
RSIPCTSRTF KCGNDICFRK QNAQCDGIVD CPDGSDEEGC GCSRSSSFLH RIVGGSDSQE
GTWPWQVSLH FVGSAYCGAS VISREWLLSA AHCFHGNRLS DPTPWTAHLG MYVQGNAKFI
SPVRRIVVHE YYNSQTFDYD IALLQLSIAW PETLKQLIQP ICIPPAGQKV RSGEKCWVTG
WGRRHEADSK GSPVLQQAEV ELIDQTVCVS TYGIITSRML CAGVMSGKSD ACKGDSGGPL
SCRRKSDGKW ILTGIVSWGH GCGRPNFPGV YTRVSSFVPW IHKYVPSLL
