ID A0A2I2ZKE7_GORGO Unreviewed; 1428 AA.
AC A0A2I2ZKE7;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN Name=PTPRK {ECO:0000313|Ensembl:ENSGGOP00000047580.1};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000047580.1, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000047580.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000047580.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000047580.1}
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: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2B subfamily. {ECO:0000256|ARBA:ARBA00006396}.
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DR EMBL; CABD030047798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030047799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030047800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030047801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030047802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030047803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030047804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030047805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030047806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSGGOT00000053238.1; ENSGGOP00000047580.1; ENSGGOG00000023696.2.
DR GeneTree; ENSGT00940000156249; -.
DR Proteomes; UP000001519; Chromosome 6.
DR Bgee; ENSGGOG00000023696; Expressed in frontal cortex and 6 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; 2.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
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; PTHR24051:SF11; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR PANTHER; PTHR24051; SUSHI DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00629; MAM; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00020; MAMDOMAIN.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 1.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00740; MAM_1; 1.
DR PROSITE; PS50060; MAM_2; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1428
FT /note="protein-tyrosine-phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014172672"
FT TRANSMEM 744..765
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..184
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 186..271
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 284..379
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 481..585
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 878..1132
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1052..1123
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1164..1427
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1340..1417
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
SQ SEQUENCE 1428 AA; 161085 MW; 2F26821FC20A7402 CRC64;
FALAFPLVLF PFPFWLCSSS FLLGGCTFDD GPGACDYHQD LYDDFEWVHV SAQEPHYLPP
EMPQGSYMIV DSSDHDPGEK ARLQLPTMKE NDTHCIDFSY LLYSQKGLNP GTLNILVRVN
KGPLANPIWN VTGFTGRDWL RAELAVSTFW PNEYQVIFEA EVSGGRSGYI AIDDIQVLSY
PCDKSPHFLR LGDVEVNAGQ NATFQCIATG RDAVHNKLWL QRRNGEDIPV AQTKNINHRR
FAASFRLQEV TKTDQDLYRC VTQSERGSGV SNFAQLIVRE PPRPIAPPQL LGVGPTYLLI
QLNANSIIGD GPIILKEVEY RMTSGSWTET HAVNAPTYKL WHLDPDTEYE IRVLLTRPGE
GGTGLPGPPL ITRTKCAEPM RTPKTLKIAE IQARRIAVDW ESLGYNITRC HTFNVTICYH
YFRGHNESKA DCLDMDPKAP QHVVNHLPPY TNVSLKMILT NPEGRKESEE TIIQTDEDVP
GPVPVKSLQG TSFENKIFLN WKEPLDPNGI ITQYEISYSS IRSFDPAVPV AGPPQTVSNL
WNSTHHVFMH LHPGTTYQFF IRASTVKGFG PATAINVTTN ISAPTLPDYE GVDASLNETA
TTITVLLRPA QAKGAPISAY QIVVEELHPH RTKREAGAME CYQVPVTYQN AMSGGAPYYF
AAELPPGNLP EPAPFTVGDN RTYQGFWNPP LAPRKGYNIY FQAMSSVEKE TKTQCVRIAT
KAAATEEPEV IPDPAKQTDR VVKIAGISAG ILVFILLLLV VILIVKKSKL AKKRKDAMGN
TRQEMTHMVN AMDRSYADQS TLHAEDPLSI TFMDQHNFSP RYENHSATAE SSRLLDVPRY
LCEGTESPYQ TGQLHPAIRV ADLLQHINLM KTSDSYGFKE EYESFFEGQS ASWDVAKKDQ
NRAKNRYGNI IAYDHSRVIL QPVEDDPSSD YINANYIDGY QRPSHYIATQ GPVHETVYDF
WRMIWQEQSA CIVMVTNLVE VGRVKCYKYW PDDTEVYGDF KVTCVEMEPL AEYVVRTFTL
ERRGYNEIRE VKQFHFTGWP DHGVPYHATG LLSFIRRVKL SNPPSAGPIV VHCSAGAGRT
GCYIVIDIML DMAEREGVVD IYNCVKALRS RRINMVQTEE QYIFIHDAIL EACLCGETAI
PVCEFKAAYF DMIRIDSQTN SSHLKDEFQT LNSVTPRLQA EDCSIACLPR NHDKNRFMDM
LPPDRCLPFL ITIDGESSNY INAALMDSYR QPAAFIVTQY PLPNTVKDFW RLVYDYGCTS
IVMLNEVDLS QGCPQYWPEE GMLRYGPIQV ECMSCSMDCD VINRIFRICN LTRPQEGYLM
VQQFQYLGWA SHREVPGSKR SFLKLILQVE KWQEECEEGE GRTIIHCLNG GGRSGMFCAI
GIVVEMVKRQ NVVDVFHAVK TLRNSKPNMV EAPVSHRILD LEGILEIS
//
