GenomeNet

Database: UniProt
Entry: A0A0G2K2N0_RAT
LinkDB: A0A0G2K2N0_RAT
Original site: A0A0G2K2N0_RAT 
ID   A0A0G2K2N0_RAT          Unreviewed;      1189 AA.
AC   A0A0G2K2N0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type {ECO:0000256|PIRNR:PIRNR000934};
DE            EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR000934};
GN   Name=Ptpn14 {ECO:0000313|Ensembl:ENSRNOP00000072308.1,
GN   ECO:0000313|RGD:1307885};
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 {ECO:0000313|Ensembl:ENSRNOP00000072308.1, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000072308.1, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000072308.1,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
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] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000072308.1}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000072308.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000934};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR000934}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649,
CC       ECO:0000256|PIRNR:PIRNR000934}.
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   RefSeq; XP_006250515.1; XM_006250453.3.
DR   RefSeq; XP_008768075.1; XM_008769853.2.
DR   RefSeq; XP_017454326.1; XM_017598837.1.
DR   AlphaFoldDB; A0A0G2K2N0; -.
DR   SMR; A0A0G2K2N0; -.
DR   STRING; 10116.ENSRNOP00000072308; -.
DR   PaxDb; 10116-ENSRNOP00000004632; -.
DR   Ensembl; ENSRNOT00000086775.2; ENSRNOP00000072308.1; ENSRNOG00000003407.8.
DR   GeneID; 305064; -.
DR   AGR; RGD:1307885; -.
DR   CTD; 5784; -.
DR   RGD; 1307885; Ptpn14.
DR   eggNOG; KOG0792; Eukaryota.
DR   GeneTree; ENSGT00940000156874; -.
DR   InParanoid; A0A0G2K2N0; -.
DR   OMA; FKKCRQY; -.
DR   OrthoDB; 3108587at2759; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000003407; Expressed in skeletal muscle tissue and 17 other cell types or tissues.
DR   ExpressionAtlas; A0A0G2K2N0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:RGD.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:RGD.
DR   GO; GO:0003712; F:transcription coregulator activity; ISO:RGD.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0001946; P:lymphangiogenesis; ISO:RGD.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:0046825; P:regulation of protein export from nucleus; ISO:RGD.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd17191; FERM_F1_PTPN14; 1.
DR   CDD; cd14599; PTPc-N14; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR014392; PTP_non-rcpt_14/21.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR45706; TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR45706:SF6; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 14; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PIRSF; PIRSF000934; Tyr-Ptase_nr14; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR000934};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW   ECO:0000256|PIRNR:PIRNR000934}; Hydrolase {ECO:0000256|PIRNR:PIRNR000934};
KW   Protein phosphatase {ECO:0000256|PIRNR:PIRNR000934};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT   DOMAIN          21..306
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          911..1182
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1092..1173
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          309..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          515..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          747..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1123
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000934-1"
SQ   SEQUENCE   1189 AA;  134786 MW;  1777868172493303 CRC64;
     MPFGLKLRRT RRYNVLSKNC FVTRIRLLDS NVIECTLSVE STGQECLEAV AQRLELRETH
     YFGLWFLSKS QQARWVELEK PLKKHLDKFA NEPLLFFGVM FYVPSVSRLQ QEATRYQYYL
     QVKKDVLEGR LRCSLEQVIR LAGLAVQADF GDYNQFDSQE FLREYVLFPM DLAMEEAALE
     ELTQKVAQEH KAHSGILPAE AELMYINEVE RLDGFGQEIF PVKDSHGNSM HLGIFFMGIF
     VRNRIGRQAV IYRWNDIGTV THSKAAILLE LIDKEETALF HTDDIENAKY ISRLFTTRHK
     FYKQNKICTE QSNSPPPIRR QPTWSRSSLP RQQPYILPPM HVQCSEHYSE THTSQDSIFP
     GNEEALYCNS HNSLDLNYLN GTVTNGSVCS VHSINSLSCS QSFIQASPVS SNLSIPGSDI
     MRADYIPSHR HSTIIVPSYR PTPDYETVMR QMKRGLLHAD SQSRSLRNLN IINTHAYNQP
     EELVYSQPEM RERHPYTVPY APQGGYGHKL VSPSDQVNPQ NSAMPSKPGA GSISHTVSTP
     ELANMQLQGA QHYSTAHMLK NYLFRPPPPY PRPRPATSTP DLASHRHKYV SGSSPDLVTR
     KVQLSVKTFQ EDSSPVVHQS LQEVSEPLTA TKHHGGGGGA VNKRHSLEVM NSMVRGMEAM
     TLKSLNIPMA RRNTLREQGP SEEAGGHDVH GLPQYHHKKT FSDATMLIHS SESEEEEEAP
     EAAPQIPELR EKVEYSAQLQ AALARIPSRP PPEYPGPRKS VSNGTLRQDQ GTLLPAMARA
     RVLRHGPAKA LSVSRAEQLA VNGASLGPSI SEPDLTSVKE RVKKEPVKER PVSEMFSLED
     SIIEREMMIR NLEKQKMTGL QAQKRPLMLA ALNGLSVARV SGREDGRHDV TRVPMDERLR
     ALKKKLEDGM VFTEYEQIPN KKANGIFSTA TLPENAERSR IREVVPYEEN RVELIPTKEN
     NTGYINASHI KVVVGGSEWH YIATQGPLPH TCHDFWQMVW EQGVNVIAMV TAEEEGGRTK
     SHRYWPKLGS KHSSATYGKF KVTTKFRTDS GCYATTGLKV KHLLSGQERT VWHLQYTDWP
     HHGCPEDVQG FLSYLEEIQS VRRHTNSVLE GVKTRHPPIV VHCSAGVGRT GVVILSELMI
     YCLEHNEKVE VPTMLRFLRE QRMFMIQTIA QYKFVYQVLV QFLQNSRLI
//
DBGET integrated database retrieval system