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TIMP4_RAT
ID   TIMP4_RAT               Reviewed;         224 AA.
AC   P81556;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Metalloproteinase inhibitor 4;
DE   AltName: Full=Tissue inhibitor of metalloproteinases 4;
DE            Short=TIMP-4;
DE   Flags: Precursor;
GN   Name=Timp4;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9503367; DOI=10.1016/s0945-053x(98)90005-1;
RA   Wu I., Moses M.A.;
RT   "Molecular cloning and expression analysis of the cDNA encoding rat tissue
RT   inhibitor of metalloproteinase-4.";
RL   Matrix Biol. 16:339-342(1998).
CC   -!- FUNCTION: Complexes with metalloproteinases (such as collagenases) and
CC       irreversibly inactivates them by binding to their catalytic zinc
CC       cofactor.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in retina, smooth muscle, skin, pancreas,
CC       skeletal muscle, heart, brain, lung, kidney and testis. Not found in
CC       cartilage, spleen and liver.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family.
CC       {ECO:0000305}.
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DR   EMBL; AABR03031919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001102863.1; NM_001109393.1.
DR   AlphaFoldDB; P81556; -.
DR   SMR; P81556; -.
DR   STRING; 10116.ENSRNOP00000010748; -.
DR   MEROPS; I35.004; -.
DR   PaxDb; P81556; -.
DR   GeneID; 680130; -.
DR   KEGG; rno:680130; -.
DR   UCSC; RGD:69077; rat.
DR   CTD; 7079; -.
DR   RGD; 69077; Timp4.
DR   VEuPathDB; HostDB:ENSRNOG00000007955; -.
DR   eggNOG; KOG4745; Eukaryota.
DR   HOGENOM; CLU_084029_0_0_1; -.
DR   InParanoid; P81556; -.
DR   OMA; EPWDNLS; -.
DR   OrthoDB; 1122531at2759; -.
DR   PhylomeDB; P81556; -.
DR   TreeFam; TF317409; -.
DR   PRO; PR:P81556; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000007955; Expressed in cerebellum and 16 other tissues.
DR   Genevisible; P81556; RN.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0030017; C:sarcomere; IDA:RGD.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0002020; F:protease binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0007417; P:central nervous system development; IEP:RGD.
DR   GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; IBA:GO_Central.
DR   GO; GO:0007219; P:Notch signaling pathway; ISO:RGD.
DR   GO; GO:0042698; P:ovulation cycle; IEP:RGD.
DR   GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR   GO; GO:0009725; P:response to hormone; IEP:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:0010033; P:response to organic substance; IBA:GO_Central.
DR   GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR   Gene3D; 2.40.50.120; -; 1.
DR   Gene3D; 3.90.370.10; -; 1.
DR   InterPro; IPR001134; Netrin_domain.
DR   InterPro; IPR001820; TIMP.
DR   InterPro; IPR008993; TIMP-like_OB-fold.
DR   InterPro; IPR015614; TIMP4.
DR   InterPro; IPR027465; TIMP_C.
DR   InterPro; IPR030490; TIMP_CS.
DR   PANTHER; PTHR11844; PTHR11844; 1.
DR   PANTHER; PTHR11844:SF26; PTHR11844:SF26; 1.
DR   Pfam; PF00965; TIMP; 1.
DR   SMART; SM00206; NTR; 1.
DR   SUPFAM; SSF50242; SSF50242; 1.
DR   PROSITE; PS50189; NTR; 1.
DR   PROSITE; PS00288; TIMP; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Metal-binding; Metalloenzyme inhibitor;
KW   Metalloprotease inhibitor; Protease inhibitor; Reference proteome;
KW   Secreted; Signal; Zinc.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..224
FT                   /note="Metalloproteinase inhibitor 4"
FT                   /id="PRO_0000034351"
FT   DOMAIN          30..156
FT                   /note="NTR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   REGION          30..33
FT                   /note="Involved in metalloproteinase-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P16035"
FT   REGION          99..100
FT                   /note="Involved in metalloproteinase-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P16035"
FT   BINDING         30
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared with metalloproteinase partner"
FT                   /evidence="ECO:0000250|UniProtKB:P16035"
FT   SITE            69
FT                   /note="Involved in metalloproteinase-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P16035"
FT   DISULFID        30..102
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   DISULFID        32..131
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   DISULFID        42..156
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   DISULFID        158..205
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   DISULFID        163..168
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   DISULFID        176..197
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   CONFLICT        85
FT                   /note="E -> G (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        171
FT                   /note="S -> T (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        180
FT                   /note="D -> N (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        186
FT                   /note="K -> M (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   224 AA;  25723 MW;  AAAF44DE30F57A8B CRC64;
     MPWSPLAALS WALVLRLLAL LWPPGRGEAC SCAPAHPQQH VCHSALVIRA KISSEKVVPA
     SEDPADTQKM IRYEIKQIKM FKGFEKAKDI QYVYTPFDSS LCGVKLETNS QKQYLLTGQI
     LSDGKVFIHL CNYIEPWEDL SLVQRESLNH HYHQNCGCQI TTCYAVPCTI SAPDECLWTD
     WLLERKLYGY QAQHYVCMKH VDGICSWYRG HLHLRKEYVD IVQP
 
 
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