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Database: UniProt
Entry: G3PAL9_GASAC
LinkDB: G3PAL9_GASAC
Original site: G3PAL9_GASAC 
ID   G3PAL9_GASAC            Unreviewed;      1231 AA.
AC   G3PAL9;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000014643.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000014643.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000014643.1}
RP   IDENTIFICATION.
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|ARBA:ARBA00001490};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 3 subfamily. {ECO:0000256|ARBA:ARBA00025789}.
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DR   AlphaFoldDB; G3PAL9; -.
DR   STRING; 69293.ENSGACP00000014643; -.
DR   Ensembl; ENSGACT00000014669.1; ENSGACP00000014643.1; ENSGACG00000011062.1.
DR   eggNOG; KOG0791; Eukaryota.
DR   GeneTree; ENSGT00940000156870; -.
DR   InParanoid; G3PAL9; -.
DR   OMA; ASNYTYR; -.
DR   TreeFam; TF351926; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000011062; Expressed in spleen and 7 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd00063; FN3; 7.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 8.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR041201; PTPRJ_TM.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR46957; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR46957:SF5; PROTEIN TYROSINE PHOSPHATASE, RECEPTOR TYPE, H; 1.
DR   Pfam; PF00041; fn3; 6.
DR   Pfam; PF18861; PTP_tm; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 8.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 5.
DR   PROSITE; PS50853; FN3; 7.
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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        875..902
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          35..110
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          112..200
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          201..287
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          288..373
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          374..460
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          461..554
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          633..721
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          947..1204
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1122..1195
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          99..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          273..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1231 AA;  136640 MW;  BF84078B2573A760 CRC64;
     LIPGTRYTIS VIAVAGDNQK KSSSCVHCAH TEPEVVRNIT VTNVTTSSIS LTWNDPKGNS
     SSYRVQWTDS VDTTSITITN LTAGVQYKIT VAAVTNEGST EGQNTSVSQY TRPGEIGTPT
     VSTNTSSISL NWTSPPGEVF KFRLEWSSNG DMRNMCTYDN FAVISELIPG TSYTISVIAI
     AGDNQTEGRA HRITAVTKPE VVRNITVANV TTSSISLKWI EPKGNSSFYR VQWTDGNVTH
     NNSVNTTSIT ITNLTAGVQY KITVAAVTNE GSTEGQNTSV SQYTRPGEIG TPTVSTNTSS
     ISLNWTSPPG EVFKFRLEWS SNGAIRNMCT YDNFAVISEL IPGTSYTISV IAVAGDNQTE
     GRAHRVTAVT KPEVVRNITV ANVTTSSISL KWIEPKGNSS SYRVQWTDGN VTHNNSVNTT
     SVTITNLTAG VQYKITVAAV TNEGNTEGQN TSVYQYTRPG EIGTPTVSTN TSSISLNWTS
     PPGEVFKFRL EWSSNGDMRN MCTYDNFAVI SELIPGTSYT ISVIAVAGDN QTEGRAHPSP
     QSQPKAVADL TVEEQNTTSV RLTWLRRGQC MQSYTKRLKV SDESIRNTPI TRFYSKINDL
     VPGKQYNISV TTETVDGTEG APIWISVCTN AGAVKDLICD GPDTTIAQVI LSWKKNNGQN
     SGFKVTVNNG ETVNYTHSCC NYTVSNLRHN TSYNLSVETQ SCGLPSRPET RLCWTGITNP
     PIPKNYQDLV VVTNKEYNKF SLQIKRGLLD SINGPITHVG VLVTQTDPGA SDLTTYVSKT
     YQEWKEQATQ VYMATVKNLT ETTVTSRSEE GPLDIEIGSE NKWGAYFNGP LEANEKYQYA
     IVLFTRLTLD NQLVTGKLLA ATKFYNFVQL PQNPVVISIA IGVTLGIFCV LLIILIGFII
     YWKSLTQNES HEPALTSGFH LSRSVAVRVE EFEAYYKKQK ADSSCGFAEE FEDMKLVGTA
     QSKTQALTLE NKPKNRYNNV LPYDSSRVKL SIIHGSPYED YINANYMPGY NSRKEYIAAQ
     GPLPATVNEF WRMIWEKNVQ TLVMLTRCNE QGRVKCEQYW DHGTKHFDKI TVTTSSEIEL
     EDWTIRDFYV KNVKTAETRL VRHFHFTAWP DHGVPQTTEL LISFRHLVRE HMDQYSRNSP
     TVVHCSAGVG RTGTFITIDR LIFQIERENL VDVYGIVHDL RMHRPLMVQT EDQYVFLNQC
     ALDIIRSRTG NNVDLIYQNS AAMSIYENID P
//
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