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Database: UniProt
Entry: A0A3Q1GFG7_9TELE
LinkDB: A0A3Q1GFG7_9TELE
Original site: A0A3Q1GFG7_9TELE 
ID   A0A3Q1GFG7_9TELE        Unreviewed;      1913 AA.
AC   A0A3Q1GFG7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=PTPRS {ECO:0000313|Ensembl:ENSAPOP00000029063.1};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000029063.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000029063.1}
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   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 2A subfamily. {ECO:0000256|ARBA:ARBA00010504}.
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DR   Ensembl; ENSAPOT00000031886.1; ENSAPOP00000029063.1; ENSAPOG00000014826.1.
DR   GeneTree; ENSGT00940000153617; -.
DR   Proteomes; UP000257200; Unplaced.
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; 8.
DR   CDD; cd05738; IgI_2_RPTP_IIa_LAR_like; 1.
DR   CDD; cd05739; IgI_3_RPTP_IIa_LAR_like; 1.
DR   CDD; cd14627; R-PTP-S-2; 1.
DR   CDD; cd14625; R-PTPc-S-1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 11.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
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; IPR003598; Ig_sub2.
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; PTHR46957; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR46957:SF1; PHOSPHATIDYLINOSITOL PHOSPHATASE PTPRQ; 1.
DR   Pfam; PF00041; fn3; 7.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF13927; Ig_3; 2.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00014; FNTYPEIII.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 8.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 3.
DR   SMART; SM00194; PTPc; 2.
DR   SMART; SM00404; PTPc_motif; 2.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   SUPFAM; SSF49265; Fibronectin type III; 5.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
DR   PROSITE; PS50853; FN3; 8.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   3: Inferred from homology;
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   Reference proteome {ECO:0000313|Proteomes:UP000257200};
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..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..1913
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018773192"
FT   TRANSMEM        1267..1290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          35..125
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          137..226
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          234..316
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          323..413
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          418..512
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          516..606
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          611..710
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          715..823
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          824..922
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          923..1018
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1023..1107
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1358..1613
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1533..1604
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1645..1904
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1822..1895
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          397..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          692..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1913 AA;  213996 MW;  B529B91D88EAE17D CRC64;
     MATSGALRLS LPLLLPVTTL LLSLLLTGSH ALSPPRFTKV PVDQIGVSGG VVSFVCQATG
     DPKPRVSWNK KGKKVNSQRI ETIEFDEGAG AVLRIQPLRA PRDENIYECV AENTEGEITV
     NAKLSIIRED LLPLGFPNID MGPQLKVVER TRTATMLCAA SGNPDPEITW YKDFLPIDPS
     ASNGRIKQLR SGALQIENSE ETDQGKYECV ASNVEGVRYS SPANLYVRVR RVPPRFSIPP
     TSQEIMPGGS VNITCVAVGS PMPYVKWMLN SEDLTPEDEM PVGRNVLELS SVRESANYTC
     VAMSSLGIIE AVAQITVKSL PKPPGTPVVT ETTATSVTIT WDSGNPDPVT YYIIQYRAKS
     PDSKYETVDD ITTTRYSIGG LYPNTEYEIR VSAVNTIGQG PPSEPVETRT GEQAPASPPR
     NIKAQILPQN TMMVQWEEPE EPNGQIKGYR VYYTMDDSQP MSLWQIHNVQ DSIITTIQSL
     VPQETYTIKV LAFTSVGDGP FSEPIHVKVL QGVPGQPSKF QVGTVSDTSI ELTWEPAYDK
     EGIINYELRY KEGNFGTQMK KMFGPTTSYV LEGLRPNTDY RFSLAAISNK GIGAFTNDIS
     HKTLQAKPSA PPQDIKCSST SSTTLLVSWR PPPLKSQNGA LAGYRVRYQV VGPSDGAGDD
     EEAMEEPATE EQVLLQRLEK WTQYRVTVSA STVNGSGPES EPLTCRTDED VPGAPPRRVE
     VEVLNSTALK VMWRSLTPGK QHGQIRGYQV HYVRVENGES RGLPLIKDVM LADAQWETDD
     TAEYEMVIGG LKPDTTYSIT VAAYTTKGDG ARSKPKLVVT KGAVPGPPYL SVAQDSETSA
     MVHWDPPDLT NGMDLQGYRL QFGRKDVSPL ATLEFAPQER EHSVDNIHQG ATYLFKISAK
     SRGGFGEEAV VDLTVPENSP GGYPQINEGS NVTCCSVQLS WKPPVLAERN GVITEYTLAY
     KEAGTGDVPR ELRLPPSQSS YVLNSLKPNS AYDVKIRAHT SIGPGPYSPP FQYRTVAFDP
     ADVPKNFTVK WATKTTVVLA WKFSESRSPY KCTVEYNRQK MDVDARQMRV LVTGLRHNTT
     YEFRVTCQES MDGGPRHRVV ARTAPLILVK KPKLDIYAEP DNIFTMSFPQ VDSKDVKNFY
     VVVVPLKKTS GTVKNLKNPD EMDMEELLRE VTPKRRSRRQ LAQLDQSKPY IIACFKRLPS
     SFTVGSDHSH SICENKPLEP DQEYVFFLLA ELNATAGKMF ATSPYTDTVV TKEQKVDPLP
     VEPGDGLIWV VGPVLAVVFI ICIVIAILLY KNRKRKESEP RTKCLLNNAD IAPHHPTDPV
     EMRRINFQTP GMMNHPPIPI SELAEHTELL KANDNLKLSQ EYESIDPGQQ FTWEHSNLEV
     NKPKNRYANV IAYDHSRVIL APIEGITGSD YINANYIDGY RKQNAYIATQ GPLPETFGDF
     WRMVWEQRAA TVVMMTRLEE KSRIKCDQYW PSRGTETYGM TQVTLLDTIE LATFCVRTFS
     LHKNGSSEKR EVRQFQFTAW PDHGVPEYPT PFLAFLRRVK TCNPPDAGPI IAHCSAGVGR
     TGCFIVIDAM LERIKHEKTV DIYGHVTLMR SQRNYMVQTE DQYSFIHDAL LEAVACGNTE
     VAARSLYSYI QKLAQVESGE HVTGMELEFK RLANSKAHTS RFISANLPCN KFKNRLVNIM
     PYETTRVCLQ PIRGLEGSDY INASFIDGYR QQKAYIATQG PLAETTEDFW RMLWENNSTI
     VVMLTKLREM GREKCHQYWP AERSARYQYF VVDPMAEYNM PQYILREFKV TDARDGQSRT
     VRQFQFTDWP EQGVPKSGEG FIDFIGQVHK TKEQFGQDGP ISVHCSAGVG RTGVFITLSI
     VLERMRYEGV VDIFQTVKML RTQRPAMVQT EDEYQFCYHA ALEYLGSFDH YAT
//
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