ID A0A096NB88_PAPAN Unreviewed; 1279 AA.
AC A0A096NB88;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN Name=PTPRJ {ECO:0000313|Ensembl:ENSPANP00000010013.3};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000010013.3, ECO:0000313|Proteomes:UP000028761};
RN [1] {ECO:0000313|Ensembl:ENSPANP00000010013.3, ECO:0000313|Proteomes:UP000028761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPANP00000010013.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 STRING; 9555.ENSPANP00000010013; -.
DR Ensembl; ENSPANT00000019803.3; ENSPANP00000010013.3; ENSPANG00000019135.3.
DR eggNOG; KOG0791; Eukaryota.
DR GeneTree; ENSGT00940000156870; -.
DR HOGENOM; CLU_001541_2_0_1; -.
DR OMA; ASNYTYR; -.
DR Proteomes; UP000028761; Chromosome 12.
DR Bgee; ENSPANG00000019135; Expressed in adult mammalian kidney and 66 other cell types or tissues.
DR ExpressionAtlas; A0A096NB88; baseline.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
DR GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
DR GO; GO:0045296; F:cadherin binding; IEA:Ensembl.
DR GO; GO:0070097; F:delta-catenin binding; IEA:Ensembl.
DR GO; GO:0045295; F:gamma-catenin binding; IEA:Ensembl.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IEA:Ensembl.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; IEA:Ensembl.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0043116; P:negative regulation of vascular permeability; IEA:Ensembl.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0050918; P:positive chemotaxis; IEA:Ensembl.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR CDD; cd00063; FN3; 5.
DR CDD; cd14615; R-PTPc-J; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 6.
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; 3.
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; 5.
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:UP000028761};
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 920..941
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..154
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 311..399
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 487..568
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 570..665
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 666..762
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 983..1240
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1158..1231
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 13..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1279 AA; 139728 MW; 312AC31DF7F629E2 CRC64;
SGVTQISSEA ASFYKLNGTG TPQVPTNTSE GGEDSGANDS LRTPEQGSNG TDGASQKTPS
ATGPSPVFDI KAVSISPTNV ILTWKSNDSA ASEYKCVVKN EMENETTVTV VYRPWCNITG
LRPGTSYVFS ITPGTGNETW GDPRVINVVT EPIPVSGLRV ALTGVRQATL SWSNGDGTAS
CRVLLEGIGS HEESTQDFAV NISGLKPGVQ YSINPYLLQS NRTEGDPLGT EGVLDASNTE
RSRAGSPTTP VHNESLLGPA DSSSSQQSRD TEVLLVELKP GTRYNATVYS QAVNGTEGQP
QTIEFRTNAI QVFDVTVVNI SATSLTLTWK ISDNESSSNY TYKIHVAGET DSFNLTVSEA
RAVISGLRSS TFYRITVCPF LGDTEGTPAF LQVYTPPGPV SDFRVTVVST TEIGLAWSSH
DAESFQIHIM CISCVREVAW GEITTNQSII IGNLFPGTKY CFEIVPEGPN GTEGASRTVC
NRTAPSAVFD IHVAYVTTTE MRLEWKSPGN ASEYVYHLVI ESKHGSNHTN TSDNVVTLQG
LIPGTLYNIT ISPEVDHVPG DPSSTTQYTR PSNVSNIDVS TSTTAATLSW QNFDDASPTY
SYCLLIEKVG NSSNATQVVT GIGITNATVT ELIPGSSYTV EIFTQVGDRI KSLEPGWKSF
CTDPASVASF DCEVVPKEPA LVLKWACPPG ANAGFELEVS SGAWDNATRL ESCSSENGTE
YRTEVTYLNF STSYNISITT VSCGKMAAPT QSTCTTGITD PPPPDGSPNI TSVSHNSVKV
KFSGFEASHG PIKAYAVILT TGEAGHPSAD VLKYTYEDFK KGASDTYVTY LIRTEEKGHS
QSLSEVLKYE IDVGNESTTL GYYNGKLEPL GSYRACVAGF TNITFHPQNH GLIDGAESYV
SFSRYSDAVS LPQDPGVICG AVFGCIFGAL VIVTVGGFIF WRKKRKDAKN NEVSFSQIKS
KLIRVENFEA YFKKQQADSN CGFAEEYEDL KLVGISQPKY AAELAENRGK NRYNNVLPYD
ISRVKLSVQT HSTDDYINAN YMPGYHSKKD FIATQGPLPN TLKDFWRMVW EKNVYAIIML
TKCVEQGRTK CEEYWPSKQA QDYGDITVAM TSEIVLPEWT IRDFTVKNIQ TSESHPLRQF
HFTSWPDHGV PDTTDLLINF RYLVRDYMKQ SPPESPILVH CSAGVGRTGT FIAIDRLIYQ
IENENTVDVY GIVYDLRMHR PLMVQTEDQY VFLNQCVLDI VRSQKDSKVD LIYQNTTAMT
IYENLAPVTT FGKTNGYIA
//
