PTP1_DICDI
ID PTP1_DICDI Reviewed; 522 AA.
AC P34137; Q556U4; Q86AJ9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Tyrosine-protein phosphatase 1;
DE EC=3.1.3.48;
DE AltName: Full=Protein-tyrosine-phosphate phosphohydrolase 1;
GN Name=ptpA1-1; Synonyms=ptp1; ORFNames=DDB_G0273097;
GN and
GN Name=ptpA1-2; Synonyms=ptp1; ORFNames=DDB_G0273817;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1423620; DOI=10.1016/0092-8674(92)90597-6;
RA Howard P.K., Sefton B.M., Firtel R.A.;
RT "Analysis of a spatially regulated phosphotyrosine phosphatase identifies
RT tyrosine phosphorylation as a key regulatory pathway in Dictyostelium.";
RL Cell 71:637-647(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: May have a role in growth and in the early stages of
CC development. Affects the timing of development.
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: Cytoplasm. Cell membrane {ECO:0000305}.
CC Note=Might be tethered to the plasma membrane.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in anterior-like cells and
CC to a lesser degree in prestalk cells.
CC -!- DEVELOPMENTAL STAGE: Expressed at a very low level in vegetative cells,
CC induced by 4 hours, maximally expressed at the tight aggregate stage
CC and through the remainder of development.
CC -!- MISCELLANEOUS: The PTPase domain is interrupted by a PTPase insert
CC which shares no homologies with other PTPase proteins.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000305}.
CC -!- CAUTION: The gene for this protein is duplicated in strains AX3 and
CC AX4. These strains contain a duplication of a segment of 750 kb of
CC chromosome 2 compared to the corresponding sequence in strain AX2.
CC {ECO:0000305}.
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DR EMBL; L07125; AAA33241.1; -; Genomic_DNA.
DR EMBL; AAFI02000011; EAL70599.1; -; Genomic_DNA.
DR EMBL; AAFI02000009; EAL70766.1; -; Genomic_DNA.
DR PIR; A44267; A44267.
DR RefSeq; XP_644525.1; XM_639433.1.
DR RefSeq; XP_644725.1; XM_639633.1.
DR AlphaFoldDB; P34137; -.
DR SMR; P34137; -.
DR STRING; 44689.DDB0185117; -.
DR PaxDb; P34137; -.
DR EnsemblProtists; EAL70599; EAL70599; DDB_G0273817.
DR EnsemblProtists; EAL70766; EAL70766; DDB_G0273097.
DR GeneID; 8618825; -.
DR GeneID; 8619151; -.
DR KEGG; ddi:DDB_G0273097; -.
DR KEGG; ddi:DDB_G0273817; -.
DR dictyBase; DDB_G0273097; ptpA1-1.
DR dictyBase; DDB_G0273817; ptpA1-2.
DR eggNOG; KOG4228; Eukaryota.
DR HOGENOM; CLU_522186_0_0_1; -.
DR InParanoid; P34137; -.
DR OMA; QYEGWPD; -.
DR PhylomeDB; P34137; -.
DR PRO; PR:P34137; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016791; F:phosphatase activity; IDA:dictyBase.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0031156; P:regulation of sorocarp development; IMP:dictyBase.
DR Gene3D; 3.90.190.10; -; 1.
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 Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Hydrolase; Membrane; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..522
FT /note="Tyrosine-protein phosphatase 1"
FT /id="PRO_0000094886"
FT DOMAIN 97..471
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 32..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..426
FT /note="PTPase insert (Asn-rich)"
FT REGION 382..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 310
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT CONFLICT 423..424
FT /note="DL -> T (in Ref. 1; AAA33241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 522 AA; 59554 MW; EFCC04A0F6AEB8BF CRC64;
MGSVESSNQM NGSIENKTNK IDISVLRPLP TRSNSSISLS SSSHSSFSRM GSLGSLPTNS
GSSSPYYNNS SFDLVDEERI KSSIYNLKNH IKCIHKIKEE FRLLEESVGP SETSEGDKKH
NTSKNRYTNI LPVNHTRVQL KKIQDKEGSD YINANYIDGA YPKQFICTQG PLPNTIADFW
RMVWENRCRI IVMLSRESEN CRIKCDRYWP EQIGGEQFSI YGNGNEVFGT YSVELVEVIQ
DPEREIITRN IRLTFEGETR DITQYQYEGW PDHNIPDHTQ PFRQLLHSIT NRQNQIIPSS
DRNVPIIVHC SAGVGRTGTF CTAVIMMKKL DHYFKQLDAT PIDQVVDPFT HLPITEYQSD
NLDLKGLGYH FKSSIYNSNG INNNNNNNLN NNNNINNNSN GSNNTPQTEP NNEEDDDDAA
ESDLKYAIMD KYNSRIDFNL FSIVLKLREQ RPGMVQQLEQ YLFCYKTILD EIYHRLNCKL
GFSLPHVNNI NNYNNYSNTT TTTTSSLAST TIIHPSTNSK LN
