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Database: UniProt
Entry: A8WUY8_CAEBR
LinkDB: A8WUY8_CAEBR
Original site: A8WUY8_CAEBR 
ID   A8WUY8_CAEBR            Unreviewed;      1247 AA.
AC   A8WUY8;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 2.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=ptp-4 {ECO:0000313|WormBase:CBG03399};
GN   ORFNames=CBG03399 {ECO:0000313|EMBL:CAP24299.2,
GN   ECO:0000313|WormBase:CBG03399}, CBG_03399
GN   {ECO:0000313|EMBL:CAP24299.2};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP24299.2, ECO:0000313|Proteomes:UP000008549};
RN   [1] {ECO:0000313|EMBL:CAP24299.2, ECO:0000313|Proteomes:UP000008549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000313|EMBL:CAP24299.2,
RC   ECO:0000313|Proteomes:UP000008549};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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};
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DR   EMBL; HE601244; CAP24299.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8WUY8; -.
DR   STRING; 6238.A8WUY8; -.
DR   WormBase; CBG03399; CBP44663; WBGene00026268; Cbr-ptp-4.
DR   eggNOG; KOG4228; Eukaryota.
DR   HOGENOM; CLU_007081_0_0_1; -.
DR   InParanoid; A8WUY8; -.
DR   OMA; FSDFWSM; -.
DR   OrthoDB; 2903434at2759; -.
DR   Proteomes; UP000008549; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd00063; FN3; 3.
DR   CDD; cd00096; Ig; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
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; 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:SF3; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
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; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   4: Predicted;
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:UP000008549};
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|SAM:Phobius}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1247
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002732073"
FT   TRANSMEM        623..647
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          135..185
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          192..294
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          299..394
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          396..497
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          718..994
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          916..985
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1009..1241
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   REGION          733..752
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1247 AA;  142010 MW;  BAE578C306DF9D3A CRC64;
     MLRKHFIVFP FLLFWNHHLV ESLSVTSKNA TEALLRCPPA ESFIRTHMAP DFETPRLVRR
     LDWFQDDSLV ASYQQGHVEG VEKELEKKKI GLDMPHISVD GHQNFHSFLN SWDKKKEKMV
     SLNIGRLADS SRQWWVADGR YQLIRPFYTL RVSPVTPEDS GTYRCRLETD PLFSSPQSTA
     TQELAVMVRP VAPSSPEIKS FTNRSITLVW THNAARAHRP ILRFSVSVRT VPFASYCPPS
     IVNFRFVMAA PSNATTVIVD NLSPYTLYAF SVRAENSAGS SDFGPETTFR TLGEPPNRAP
     QIQKIRNVTS ECVEVTVTPP DEMNGELEKY LVLIQAVNET NPRKMTFDKP TSTPLTICAL
     TPSSEYALAI EADNGFGTSP QATLVFRTED SVPNWSPSTI KTTPVVGKPE IIVLWLAPPM
     NATEKVVKYH LYYKANNEDQ WKIEHLNVNP NEVKSKMFKY RLVDLNPNTL YRIRVSASTS
     KGEGSQSADS LAQTDVGEPG TVIFKDLNFD CKNGVKLSWN YEPSVNSKKS PTFTVKITNQ
     TTSLQFNTTR QTLDIIDLSL YDEYSLRIIV LERSTIDNTT ILIGKYSDNH RFILKDKCAY
     QSSFCSPGEK CAKLTSSAAN PQYISVLIVI FAIIIFAFIC FIIVHFARGS MNFKHLLKKK
     EKCVYLEEIS PLVYGRLNRS DMISMKCYCL DSAGQEDIPV ELFYGYVEDL NRNDALKFKT
     QFQILETQTS GIDQADSGES TSSADENSQK NRYNNIGAME ATRIRLNSPT GNDYINANYV
     DSCNERNAYI ATQAPLPSTF SDFWSMIWQE RSNVIVCITN MVEDGKVKKG MSYFPNSIFR
     FQRKCDQYWP SVPDSPQNFG NYQVTLISES TNAHFSHRVL DLKIAKSVPA AERKIHQLHF
     VGWPDHGVPS SVFPLLNFIH YASDIHSTGP VVVHCSAGVG RSGSYILVDS MRRHLISFRR
     LNVQGHLTHM RRQRAKLVQT LEQYIFCHEA IRQLIRHGIT RVHSDLFMRY LHYLSEENLN
     GKTRMQLQYE DVCECKHQPR CLIDSDVLTL PGYHRSDEFM VGSWSHECEE LWKLIWKRKV
     QTIVVLNQRD SFWRKLHLCE DIQLQHGDNF VLMQREDQQL CVRIMNVARS DLDADFWREI
     ENVQKQRITY HDAPLLILAQ KFPPNASSPT DSTSTLSLSM LFNDDSSLAF SICAATTLAC
     QLETTGCVDV VQVLSSYTEI QCGIFSSKQE IEIIYEKISQ LVEGTRV
//
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