ID A0A452EJP2_CAPHI Unreviewed; 756 AA.
AC A0A452EJP2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 12 {ECO:0000256|PIRNR:PIRNR000932};
DE EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR000932};
GN Name=PTPN12 {ECO:0000313|Ensembl:ENSCHIP00000012158.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000012158.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000012158.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000012158.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Dephosphorylates a range of proteins, and thereby regulates
CC cellular signaling cascades. {ECO:0000256|PIRNR:PIRNR000932}.
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:PIRNR000932};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000932}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class 4 subfamily. {ECO:0000256|ARBA:ARBA00034734,
CC ECO:0000256|PIRNR:PIRNR000932}.
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DR EMBL; LWLT01000003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452EJP2; -.
DR Ensembl; ENSCHIT00000019948.1; ENSCHIP00000012158.1; ENSCHIG00000014032.1.
DR GeneTree; ENSGT00940000156909; -.
DR Proteomes; UP000291000; Chromosome 4.
DR Bgee; ENSCHIG00000014032; Expressed in adrenal gland and 18 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR012266; PTN12.
DR InterPro; IPR047170; PTN12/18/22.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR45983; TYROSINE PHOSPHATSE N18, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR45983:SF3; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 12; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF000932; Tyr-Ptase_nr12; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR000932};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000932};
KW Protein phosphatase {ECO:0000256|PIRNR:PIRNR000932};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000}.
FT DOMAIN 28..267
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 207..275
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 478..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 756 AA; 85022 MW; 896F0DBD925B34DF CRC64;
MEQVEILRKF IQRVQAMKSP DHNGEDNFAR DFMRLRRLST KYRTEKIYPT ATGEKEENVK
KNRYKDILPF DHSRVKLTLK TPSQDSDYIN ANFIKGVYGP KAYVATQGPL ANTVIDFWRM
IWEYNVVIIV MACREFEMGR KKCERYWPLF GEDPITFAPF KISCEAEQAR TDYFIRTLLL
EFQNESRRLY QFHYVNWPDH DVPSSFDSIL DMISLMRKYQ EHEDVPICIH CSAGCGRTGA
ICAIDYTWNL LKAGEQYELV HRAIAQLFEK QLQLYEIHGT QKITDGVNEV NTENMISSID
HDKQDSPPPK PPRTRSCLVE GDAKEEILQP PEPHPVPPIL TPSPPSAFPT VTTVWQDNDR
YHPKPVLHMV SSEQPSTDLN RNYNKSTELT GKNESTIEQI DKKLERNLSF EIKKVPLQEG
PRSFDGNTLL NRGHAIKIKS ASASPCTVDK ISKSQELSSR DLKVDDISQN SCVDCNATQS
NKDPIILPEA SQKNSDTPPR PDHLPLDGKG HLTWSFHGPE NTLPMPDSSE GKSSDIHCQT
MKTVSSTPSP TIQAETHDLA DHHDSSPLFR APLSFTNPLH SDDSDSDERN SDGTVTKNKT
SISTASATVS AATSSISTRK VLPMSIARHD IAGTIHSGAE KDVDVSEDSP PPLPERTPES
FVLANEHNTS VRAEWSELQN QEQSEQKIPE GLITSGSETC DHPARGIHTE TCTECPPTFS
NKKDQLSESP TEATEIGFGN RCGKPKGPRD PPSEWT
//
