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TMPS5_HUMAN
ID   TMPS5_HUMAN             Reviewed;         457 AA.
AC   Q9H3S3;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Transmembrane protease serine 5;
DE            EC=3.4.21.-;
DE   AltName: Full=Spinesin;
GN   Name=TMPRSS5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=11741986; DOI=10.1074/jbc.m103645200;
RA   Yamaguchi N., Okui A., Yamada T., Nakazato H., Mitsui S.;
RT   "Spinesin/TMPRSS5, a novel transmembrane serine protease, cloned from human
RT   spinal cord.";
RL   J. Biol. Chem. 277:6806-6812(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, VARIANTS VAL-31; GLN-46; VAL-249; SER-317;
RP   SER-337 AND LEU-369, AND CHARACTERIZATION OF VARIANTS SER-317 AND LEU-369.
RX   PubMed=17918732; DOI=10.1002/humu.20617;
RA   Guipponi M., Toh M.-Y., Tan J., Park D., Hanson K., Ballana E., Kwong D.,
RA   Cannon P.Z.F., Wu Q., Gout A., Delorenzi M., Speed T.P., Smith R.J.H.,
RA   Dahl H.-H.M., Petersen M., Teasdale R.D., Estivill X., Park W.J.,
RA   Scott H.S.;
RT   "An integrated genetic and functional analysis of the role of type II
RT   transmembrane serine proteases (TMPRSSs) in hearing loss.";
RL   Hum. Mutat. 29:130-141(2008).
CC   -!- FUNCTION: May play a role in hearing. {ECO:0000269|PubMed:17918732}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Brain-specific. Predominantly expressed in neurons,
CC       in their axons, and at the synapses of motoneurons in the spinal cord.
CC   -!- DISEASE: Note=Defects in TMPRSS5 may be a cause of deafness.
CC       {ECO:0000269|PubMed:17918732}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; AB028140; BAB20375.1; -; mRNA.
DR   EMBL; AP002436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP003402; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS44735.1; -.
DR   RefSeq; NP_001275678.1; NM_001288749.1.
DR   RefSeq; NP_001275679.1; NM_001288750.1.
DR   RefSeq; NP_001275680.1; NM_001288751.1.
DR   RefSeq; NP_001275681.1; NM_001288752.1.
DR   RefSeq; NP_110397.2; NM_030770.3.
DR   AlphaFoldDB; Q9H3S3; -.
DR   SMR; Q9H3S3; -.
DR   BioGRID; 123345; 54.
DR   IntAct; Q9H3S3; 2.
DR   STRING; 9606.ENSP00000299882; -.
DR   MEROPS; S01.313; -.
DR   GlyGen; Q9H3S3; 5 sites.
DR   PhosphoSitePlus; Q9H3S3; -.
DR   BioMuta; TMPRSS5; -.
DR   DMDM; 296452845; -.
DR   MassIVE; Q9H3S3; -.
DR   PaxDb; Q9H3S3; -.
DR   PeptideAtlas; Q9H3S3; -.
DR   PRIDE; Q9H3S3; -.
DR   ProteomicsDB; 80747; -.
DR   Antibodypedia; 2582; 326 antibodies from 31 providers.
DR   DNASU; 80975; -.
DR   Ensembl; ENST00000299882.11; ENSP00000299882.5; ENSG00000166682.13.
DR   GeneID; 80975; -.
DR   KEGG; hsa:80975; -.
DR   MANE-Select; ENST00000299882.11; ENSP00000299882.5; NM_030770.4; NP_110397.2.
DR   UCSC; uc001poc.6; human.
DR   CTD; 80975; -.
DR   DisGeNET; 80975; -.
DR   GeneCards; TMPRSS5; -.
DR   HGNC; HGNC:14908; TMPRSS5.
DR   HPA; ENSG00000166682; Group enriched (brain, choroid plexus).
DR   MIM; 606751; gene.
DR   neXtProt; NX_Q9H3S3; -.
DR   OpenTargets; ENSG00000166682; -.
DR   PharmGKB; PA37920; -.
DR   VEuPathDB; HostDB:ENSG00000166682; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000159163; -.
DR   InParanoid; Q9H3S3; -.
DR   OMA; CSERWNS; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; Q9H3S3; -.
DR   TreeFam; TF351678; -.
DR   PathwayCommons; Q9H3S3; -.
DR   SignaLink; Q9H3S3; -.
DR   BioGRID-ORCS; 80975; 4 hits in 1067 CRISPR screens.
DR   ChiTaRS; TMPRSS5; human.
DR   GenomeRNAi; 80975; -.
DR   Pharos; Q9H3S3; Tbio.
DR   PRO; PR:Q9H3S3; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q9H3S3; protein.
DR   Bgee; ENSG00000166682; Expressed in tibial nerve and 107 other tissues.
DR   ExpressionAtlas; Q9H3S3; baseline and differential.
DR   Genevisible; Q9H3S3; HS.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0008233; F:peptidase activity; IMP:UniProtKB.
DR   GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IMP:UniProtKB.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001190; SRCR.
DR   InterPro; IPR017448; SRCR-like_dom.
DR   InterPro; IPR036772; SRCR-like_dom_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF15494; SRCR_2; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF56487; SSF56487; 1.
DR   PROSITE; PS00420; SRCR_1; 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; Serine protease; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..457
FT                   /note="Transmembrane protease serine 5"
FT                   /id="PRO_0000088694"
FT   TOPO_DOM        1..49
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        71..457
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          112..207
FT                   /note="SRCR"
FT   DOMAIN          218..453
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        258
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        308
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        405
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   SITE            217..218
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        319
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        135..196
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        148..206
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        209..328
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        243..259
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        342..411
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        374..390
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        401..429
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   VARIANT         31
FT                   /note="D -> V (in patients with sporadic hearing loss)"
FT                   /evidence="ECO:0000269|PubMed:17918732"
FT                   /id="VAR_038005"
FT   VARIANT         46
FT                   /note="R -> Q (in dbSNP:rs11601425)"
FT                   /evidence="ECO:0000269|PubMed:17918732"
FT                   /id="VAR_038006"
FT   VARIANT         125
FT                   /note="V -> M (in dbSNP:rs7939917)"
FT                   /id="VAR_038007"
FT   VARIANT         249
FT                   /note="A -> V (in dbSNP:rs1263487635)"
FT                   /evidence="ECO:0000269|PubMed:17918732"
FT                   /id="VAR_038008"
FT   VARIANT         317
FT                   /note="A -> S (in patients with sporadic hearing loss; no
FT                   detectable proteolytic activity in a yeast-based protease
FT                   assay)"
FT                   /evidence="ECO:0000269|PubMed:17918732"
FT                   /id="VAR_038009"
FT   VARIANT         337
FT                   /note="P -> S"
FT                   /evidence="ECO:0000269|PubMed:17918732"
FT                   /id="VAR_038010"
FT   VARIANT         369
FT                   /note="F -> L (reduced proteolytic activity in a yeast-
FT                   based protease assay; dbSNP:rs7110736)"
FT                   /evidence="ECO:0000269|PubMed:17918732"
FT                   /id="VAR_038011"
FT   CONFLICT        428
FT                   /note="G -> A (in Ref. 1; BAB20375)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   457 AA;  49560 MW;  64406AB4985C4637 CRC64;
     MSLMLDDQPP MEAQYAEEGP GPGIFRAEPG DQQHPISQAV CWRSMRRGCA VLGALGLLAG
     AGVGSWLLVL YLCPAASQPI SGTLQDEEIT LSCSEASAEE ALLPALPKTV SFRINSEDFL
     LEAQVRDQPR WLLVCHEGWS PALGLQICWS LGHLRLTHHK GVNLTDIKLN SSQEFAQLSP
     RLGGFLEEAW QPRNNCTSGQ VVSLRCSECG ARPLASRIVG GQSVAPGRWP WQASVALGFR
     HTCGGSVLAP RWVVTAAHCM HSFRLARLSS WRVHAGLVSH SAVRPHQGAL VERIIPHPLY
     SAQNHDYDVA LLRLQTALNF SDTVGAVCLP AKEQHFPKGS RCWVSGWGHT HPSHTYSSDM
     LQDTVVPLFS TQLCNSSCVY SGALTPRMLC AGYLDGRADA CQGDSGGPLV CPDGDTWRLV
     GVVSWGRGCA EPNHPGVYAK VAEFLDWIHD TAQDSLL
 
 
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