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Database: UniProt
Entry: A0A401T302_CHIPU
LinkDB: A0A401T302_CHIPU
Original site: A0A401T302_CHIPU 
ID   A0A401T302_CHIPU        Unreviewed;       463 AA.
AC   A0A401T302;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=M-phase inducer phosphatase {ECO:0000256|RuleBase:RU368028};
DE            EC=3.1.3.48 {ECO:0000256|RuleBase:RU368028};
GN   ORFNames=chiPu_0015522 {ECO:0000313|EMBL:GCC37022.1};
OS   Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC   Chiloscyllium.
OX   NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC37022.1, ECO:0000313|Proteomes:UP000287033};
RN   [1] {ECO:0000313|EMBL:GCC37022.1, ECO:0000313|Proteomes:UP000287033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA   Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA   Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA   Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA   Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT   "Shark genomes provide insights into elasmobranch evolution and the origin
RT   of vertebrates.";
RL   Nat. Ecol. Evol. 2:1761-1771(2018).
CC   -!- FUNCTION: Functions as a dosage-dependent inducer in mitotic control.
CC       Tyrosine protein phosphatase required for progression of the cell
CC       cycle. {ECO:0000256|RuleBase:RU368028}.
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         ECO:0000256|RuleBase:RU368028};
CC   -!- SIMILARITY: Belongs to the MPI phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00011065, ECO:0000256|RuleBase:RU368028}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GCC37022.1}.
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DR   EMBL; BEZZ01000926; GCC37022.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401T302; -.
DR   STRING; 137246.A0A401T302; -.
DR   OMA; NSAPAQM; -.
DR   Proteomes; UP000287033; Unassembled WGS sequence.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR   GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; IEA:InterPro.
DR   CDD; cd01530; Cdc25; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   InterPro; IPR000751; MPI_Phosphatase.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   PANTHER; PTHR10828:SF48; M-PHASE INDUCER PHOSPHATASE 2; 1.
DR   PANTHER; PTHR10828; M-PHASE INDUCER PHOSPHATASE DUAL SPECIFICITY PHOSPHATASE CDC25; 1.
DR   Pfam; PF06617; M-inducer_phosp; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   PRINTS; PR00716; MPIPHPHTASE.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU368028};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618,
KW   ECO:0000256|RuleBase:RU368028};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368028};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776, ECO:0000256|RuleBase:RU368028};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW   ECO:0000256|RuleBase:RU368028};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287033}.
FT   DOMAIN          312..421
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   REGION          47..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   463 AA;  53254 MW;  091490F4D303B855 CRC64;
     MDSPSPMDEK AINETFEKAI LESGKVNTKK IPIRRINSLP MRLLGSSPAL KSSQCNSLDS
     EVFHEGSGTP STEENKENEG FEFKKPVHPV SRNRLCTFSS GSRQDQRPNS APALMFSPSI
     SDVSTDVSSP ILLRKSSLTS SIDDEDDGFL ELLDEDIEND ADVPSGMASL LTAPLVARKE
     ISPETLDEAP HKWSYADNVK SPNLAPEMRS ILKRVDRPKD EETPVKNKRR RSLAGITEET
     SAEKVKQHSL LRSKSFCDAE IEKVLQIDDC RRMIGDFTKP YILPTVEGRH QELQYVTAEM
     VIQLVNGEFD EFVEQFLLFD CRYPYEYEGG HIKGALNLHM EEEVESFLLK KPIVPVDEAK
     RVIIIFHCEF SSERAPRMCR FLREKDREVN GTDYPKLHYP ELYILKGGYK EFFPKFKLYC
     EPQSYRPMNH EDFKEDLRKF RFKSRTWAGE RSKRDMYSRL KKL
//
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