ID E4XAH3_OIKDI Unreviewed; 1677 AA.
AC E4XAH3;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN ORFNames=GSOID_T00005229001 {ECO:0000313|EMBL:CBY08646.1};
OS Oikopleura dioica (Tunicate).
OC Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC Oikopleuridae; Oikopleura.
OX NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY08646.1};
RN [1] {ECO:0000313|EMBL:CBY08646.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21097902; DOI=10.1126/science.1194167;
RA Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA Roest Crollius H., Wincker P., Chourrout D.;
RT "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT pelagic tunicate.";
RL Science 330:1381-1385(2010).
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 2B subfamily. {ECO:0000256|ARBA:ARBA00006396}.
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DR EMBL; FN653032; CBY08646.1; -; Genomic_DNA.
DR InParanoid; E4XAH3; -.
DR Proteomes; UP000001307; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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 CDD; cd00047; PTPc; 2.
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; 3.
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; 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; PTHR19134:SF533; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00629; MAM; 1.
DR Pfam; PF00102; Y_phosphatase; 3.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00194; PTPc; 3.
DR SMART; SM00404; PTPc_motif; 3.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 3.
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; 3.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50060; MAM_2; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 3.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 3.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000001307};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1677
FT /note="protein-tyrosine-phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003190134"
FT DOMAIN 39..181
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 183..274
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 281..383
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 394..489
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 493..598
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 898..1152
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1070..1143
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1182..1449
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1367..1440
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1445..1671
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1589..1662
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 832..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1677 AA; 188255 MW; 839DC61108852DD2 CRC64;
MLGQTAWTTL LWILAAFGNG NGLVAAQQIS RLYTPLNTGS CKFDRADPWC NFRQGTEDEF
DWEMDETDRA SGFVFVDTNV HEQGQQARLF TPSIDNKDTH CVSFDFKITG HGEISVYVIR
DFFVYSQPVW SSQSITTEWT TVQLALSPQS YKLVFEGRIL SRSNGLIALD NINVQYQSCR
EAPHFLRLGD TEVNEGQSAE LQCIANGDAS WGQNIRLQKF SSGMEEKIFR SHNMVNFQSA
KFIWPAIGTA DADKIRCVAS NKTAAGVSNY AELKVRRPPV PIRAPEVDSA GPTHLIVRLN
VDPNNHETFT GDGPVSNIEF RYKKVESAWE DGHDVSLATY NGTYRIWHLE PDTLYMLCVV
LERPGPGGTG KPGPCLEIRT KCAKPMPLTQ ITVSPYKGQV VSETAQSNYA DNLLVRWAKP
TPRHAGCRTW GYVLKWRQVG GFWKTQEPES NRTIISNLRA DTPYEVQVSI RNMVGTTDSL
VIPTKTNDGL PEPIPSFKIK VITTEQSIIV QWPHPAVPNG DILAFKLRYS FFDAFDGPRD
FHPGPPFQGE FQVPASRNVY EIANLPPGTT YNLTLSAKTS AGFGRPSEFT GTTKIGSPKW
TSAYDAKEFS TSEDIVVTLR GADGNGAPVS HYNVVVENAD NNTGRRRRSL SSKNGCFDRS
ISYDTYIKTG AEYYFAAEID QRYFEERQME IPFRVGDNNT YNGFRNAPLP PGKKVSIWVQ
AVSIQPGCNF SRGKHCDRNV KCQVVATRGV KPPPPPVEDM NNSNSERIYT EETTLKEGEL
ATTSIMLYGG VSVALLFLLF VFVGSVVCFR RRALAMGPER YRVASPTDFG NRTDGMYSDH
SDVKKPPSSY PTEKTPLMPD LVDYPSSSRK SEAEDFAVRV EDFPIHVSQM RSSRTYSFAD
EFETLPEGNT ASWDVAQKPE NIQKNRYTNI LPYDHSRVVL RSNTQINSSG DYINASWISG
YGLRYVAAQG PTETTIPDFW HAVWQENIRL VIMVTGLVEV GRRKCHQYWP NEIRGIERYG
NFSVELISEQ ILAHYTLREF KICLGNLEPR IIRQMQFQSW PDHGVPTRPT GLLHFVRRSA
QLNPDYNPVL VHCSAGSGRS GCFIVLDWML RMADSEGLLD IYNTVKELRN KRVNMVANLE
QYIFLHDSLL EAVLCGETGV QAMDLSSHYD NLITVTGGGA PIQEEFETLA VLTPRLTTEE
CQTARLARNR VKNRFQDVLP ADRDLPYLIT PDPAGSDPSH NYINAVFADS FLVKRDLIIT
QMPLPHTVGD FWRLVHDYSV SVVVMLNDAS ETDETCANYW PAEQTSETYS AFTVESLDKS
DEIELISRTL KLTNYYRSND PAKEVKLLQL SNWPAGQPVP SSRNAVLRLV SLIDQHRSTL
PPGSRVLLHC VAGAGKSGTF ASCYNVIQQL KTLQTADVFS SVLQLRAVRP QLVETLEQYR
FIYEVAMEYA DCEAMSGSDP SHNYINAVFA DSFLVKRDLI ITQMPLPHTV GDFWRLVHDY
SVSVVVMLND ASETDETCAN YWPAEQTSET YSAFTVESLD KSDEIELISR TLKLTNYYRS
NDPAKEVKLL QLSNWPAGQP VPSSRNAVLR LVSLIDQHRS TLPPGSRVLL HCVAGAGKSG
TFASCYNVIQ QLKTLQTADV FSSVLQLRAV RPQLVETLEQ YRFIYEVAME YADCEAM
//
