ID E7F3D4_DANRE Unreviewed; 589 AA.
AC E7F3D4; A0A8N7XJL7; S6CNK8;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 2.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type {ECO:0000256|PIRNR:PIRNR000929};
DE EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR000929};
GN Name=ptpn6 {ECO:0000313|EMBL:CBX19677.1,
GN ECO:0000313|Ensembl:ENSDARP00000105983,
GN ECO:0000313|RefSeq:XP_009290704.1,
GN ECO:0000313|ZFIN:ZDB-GENE-030131-7513};
GN Synonyms=fj22f05 {ECO:0000313|RefSeq:XP_009290704.1}, Hcph
GN {ECO:0000313|RefSeq:XP_009290704.1}, SHP1
GN {ECO:0000313|RefSeq:XP_009290704.1}, wu:fj22f05
GN {ECO:0000313|RefSeq:XP_009290704.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|EMBL:CBX19677.1};
RN [1] {ECO:0000313|EMBL:CBX19677.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22412924; DOI=10.1371/journal.pone.0032777;
RA Liongue C., O'Sullivan L.A., Trengove M.C., Ward A.C.;
RT "Evolution of JAK-STAT pathway components: mechanisms and role in immune
RT system development.";
RL PLoS ONE 7:E32777-E32777(2012).
RN [2] {ECO:0000313|Ensembl:ENSDARP00000105983, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000105983};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000313|Ensembl:ENSDARP00000146029}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000105983};
RG Ensembl;
RL Submitted (APR-2018) to UniProtKB.
RN [4] {ECO:0000313|RefSeq:XP_009290704.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_009290704.1};
RG RefSeq;
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|ARBA:ARBA00001490,
CC ECO:0000256|PIRNR:PIRNR000929};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000929}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class 2 subfamily. {ECO:0000256|ARBA:ARBA00010750,
CC ECO:0000256|PIRNR:PIRNR000929}.
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DR EMBL; BX511250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; LO017669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN001513; CBX19677.1; -; mRNA.
DR RefSeq; XP_009290704.1; XM_009292429.3.
DR PaxDb; 7955-ENSDARP00000027536; -.
DR Ensembl; ENSDART00000126617.4; ENSDARP00000105983.2; ENSDARG00000089043.5.
DR Ensembl; ENSDART00000182722.1; ENSDARP00000146029.1; ENSDARG00000089043.5.
DR GeneID; 335573; -.
DR AGR; ZFIN:ZDB-GENE-030131-7513; -.
DR CTD; 5777; -.
DR ZFIN; ZDB-GENE-030131-7513; ptpn6.
DR eggNOG; KOG0790; Eukaryota.
DR OrthoDB; 2911650at2759; -.
DR TreeFam; TF351632; -.
DR Proteomes; UP000000437; Chromosome 16.
DR Bgee; ENSDARG00000089043; Expressed in spleen and 19 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071310; P:cellular response to organic substance; IEA:UniProt.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IMP:ZFIN.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR CDD; cd14606; PTPc-N6; 1.
DR CDD; cd09931; SH2_C-SH2_SHP_like; 1.
DR CDD; cd10340; SH2_N-SH2_SHP_like; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR012152; Tyr_Pase_non-rcpt_typ-6/11.
DR PANTHER; PTHR46257; TYROSINE-PROTEIN PHOSPHATASE CORKSCREW; 1.
DR PANTHER; PTHR46257:SF4; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 6; 1.
DR Pfam; PF00017; SH2; 2.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF000929; Tyr-Ptase_nr_6; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00252; SH2; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF55550; SH2 domain; 2.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR000929};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000929};
KW Protein phosphatase {ECO:0000256|PIRNR:PIRNR000929};
KW Receptor {ECO:0000313|EMBL:CBX19677.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}.
FT DOMAIN 4..100
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 110..210
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 247..518
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 433..509
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 539..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 456
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000929-1"
FT BINDING 422
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000929-2"
FT BINDING 503
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000929-2"
SQ SEQUENCE 589 AA; 67005 MW; 0A94CE330E4A6F19 CRC64;
MVRWFHRDLS GLDAEAVLKS RGVHGSFLAR PSKKNVGDFS LSVRVGEIIT HIRIQNTGDY
YDLYGGEKFA TLAELVEYYT GDHGTLQDKD GTVIELKYPL NCSDPTTERW YHGHLSGPNA
EKLLRERNEP GTFLVRESLS KPGDFVLSAL TDDQTSSGRR VSHIKIMCNN DRYTVGGKDQ
FDNLTDLVEH FKRVGIEELS GTMVYLKQPY YSTRLNAADI QSRVNQLDQT SEREKMDGAD
KKIKAGFWEE FDALQKLETK VTKSRDEGMR PENKSKNRYK NILPFDETRV ILENADPNVV
GSDYINANYV INKLMVTNPQ KTYIACQGCL ATTVDDFWQM MWQEDSRVIV MTTREVEKGR
NKCVPYWPTT EGESKEVGRY VVKLLSEMDA ADYKVRVVEL SAPHRNEAPR KIWHFQYLSW
PDHGVPQEPG GVLSFLDQVN RKQEELRSSA PIVIHCSAGI GRTGTIVVID MLIDSIDAKG
LDCDIDIQKC IMMVRDQRSG MVQTEAQYKF IYLAVLQYIE STKVTRRAIM ETETEYGNLS
IQSKHPKASR KASSKKNEDV YENLGAKGKK DVKKQKSEEK KGGGSVRKR
//
