ID   PTPRG_CHICK             Reviewed;        1422 AA.
AC   Q98936;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=Receptor-type tyrosine-protein phosphatase gamma;
DE            Short=Protein-tyrosine phosphatase gamma;
DE            Short=R-PTP-gamma;
DE            EC=3.1.3.48;
DE   Flags: Precursor;
GN   Name=PTPRG;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain, and Kidney;
RA   Qinghua X., Xiaojun G., Cong S., Zong S.M., Jong Y.J., Chan J., Wang L.-H.;
RL   Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10044};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 5 subfamily. {ECO:0000305}.
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DR   EMBL; U38349; AAB16910.1; -; mRNA.
DR   PIR; T42636; T42636.
DR   AlphaFoldDB; Q98936; -.
DR   SMR; Q98936; -.
DR   STRING; 9031.ENSGALP00000043685; -.
DR   GlyCosmos; Q98936; 9 sites, No reported glycans.
DR   PaxDb; 9031-ENSGALP00000011605; -.
DR   VEuPathDB; HostDB:geneid_374208; -.
DR   eggNOG; KOG0382; Eukaryota.
DR   eggNOG; KOG0789; Eukaryota.
DR   InParanoid; Q98936; -.
DR   PhylomeDB; Q98936; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd03122; alpha_CARP_receptor_like; 1.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd17670; R-PTP-G-2; 1.
DR   CDD; cd17667; R-PTPc-G-1; 1.
DR   Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR   InterPro; IPR041887; Alpha_CARP_receptor-type.
DR   InterPro; IPR001148; CA_dom.
DR   InterPro; IPR036398; CA_dom_sf.
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; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR19134:SF449; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE GAMMA; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00194; PTPc; 2.
DR   SMART; SM00404; PTPc_motif; 2.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protein phosphatase;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..1422
FT                   /note="Receptor-type tyrosine-protein phosphatase gamma"
FT                   /id="PRO_0000025443"
FT   TOPO_DOM        20..742
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        743..768
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        769..1422
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          58..321
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   DOMAIN          349..448
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          825..1096
FT                   /note="Tyrosine-protein phosphatase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   DOMAIN          1127..1387
FT                   /note="Tyrosine-protein phosphatase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          541..708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1396..1422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..590
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..614
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..649
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        688..708
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1037
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT                   ECO:0000255|PROSITE-ProRule:PRU10044"
FT   BINDING         1005
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1037..1043
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1081
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            1328
FT                   /note="Ancestral active site"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        359
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        444
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        620
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        632
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        640
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        728
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        78..261
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1422 AA;  159767 MW;  DD484055993DA74F CRC64;
     MRRLLQPCWW IFFLKITSSV LHDVVCFPAL TEGYVGSLHE SRHGSSVQIR RRKASGDPYW
     GYSGTYGPEH WVTSSEKCGG SHQSPIDIVD HQAHVLYEYQ ELQLDGFDNE SSNKTWMKNT
     GKTVAILLKD DYFVSGAGLP GRFKAEKVEF HWGQSNGSAG SEHSINGKRF PVEMQIYFYN
     PDDFDSFGTA VLENREVGAM AVFFQVSQRD NSALDPIIRG LKGVVHHEKE TFLDPFVLRD
     LLPTSLGSYY RYTGSLTTPP CSEIVEWIIF RKPVPISYHQ LEAFYSIFTT EQQDHVKSVE
     YLRNNFRPQQ RLNNRKVSKS AVKDAWSQDM TDILENPLGT EASKACSTPP VNMKVQPVNR
     TALLVTWNQP ETIYHPPIMN YMISYSWTKN EDEKEKTFTK DSDKDLKAII SHVSPDILYL
     FRVQAVCRNE MRSDFSQTML FQANTTRIFE GTRIVKTGVP TASPASSADM APISSGSSTW
     TSSGLPFSFV SMATGMGPSS SGSQATVASV VTSTLLAGLG FSGSSISSFP SSVWPTRLPT
     AAAPTKQAGR PVVATTEPAA ASPGPERDSA LTKDGEGAEE GEKDEKSESE DGEREHEEED
     EKEAEKKEKS RATAAAEARN STEPSVATAS PNWTAEEEGN KTVSGEEPNQ NVVPKAGRPE
     EESFTDADTQ PQPLPSTQVP PAFTDELYLE KIPRRPETTR KPLPKDNRFL EEYPSDNKFI
     TINPADKNSS SMATRPSPGK MEWIIPLIVV SALTFVCLIL LIAVLVYWRK CFQTAHFYVE
     DSSSPRVVPN ESIPIIPIPD DMEAIPVKQF VKHISELYSN NQHGFSEDFE EVQRCTADMN
     ITAEHSNHPD NKHKNRYINI LAYDHSRVKL RPLPGKDSKH SDYINANYVS GYNKAKAYIA
     TQGPLKSTFE DFWRMIWAQH TGIIVMITNL VEKGRRKCDQ YWPTENSEEY GNIIVTLKST
     NIHACYTVRP LHGQEHKDEK GSERKPKGRQ NERTVIQYHY TQWPDMGVPE YALPVLTFVR
     RSSAARTPHM GPVVVHCSAG VGRTGTYIVI DSMLQQIKDK STVNVLGFLK HIRTQRNYLV
     QTEEQYIFIH DALLEAILGK ETEVSANQLH SYVNSILIPG IGGKTRLEKQ FKLVTQCNAK
     YVECFSAQKD CNKEKNRNSS VVPSERARVG LAPLPGMKGT DYINASYIMG YYRSNENVIT
     QHPLPHTTKD FWRMIWDHNA QIIVMLPDNQ SLAEDEFVYW PSREESMNCE AFTVTLISKD
     RLCLSNEEQI IIHDFILEAT QDDYVLEVRH FQCPKWPNPD APISSTFELI NVIKEEALTR
     DGPTIVHDEY GAVSAGTLCA LTTLSQQLEN ENAVDVFQVA KMINLMRPGV FTDIEQYQFL
     YKAMLSLVST KENGNGPMTL DKNGAVMASD ESDPAESMES LV
//