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
//