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MYPT1_CHICK
ID   MYPT1_CHICK             Reviewed;        1004 AA.
AC   Q90623; Q10727; Q90624;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 12A;
DE   AltName: Full=130 kDa myosin-binding subunit of smooth muscle myosin phosphatase;
DE   AltName: Full=Myosin phosphatase-targeting subunit 1;
DE            Short=Myosin phosphatase target subunit 1;
DE   AltName: Full=PP1M subunit M110;
DE   AltName: Full=Protein phosphatase myosin-binding subunit;
GN   Name=PPP1R12A; Synonyms=MBS, MYPT1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PARTIAL PROTEIN SEQUENCE,
RP   FUNCTION, SUBUNIT, INTERACTION WITH MYOSIN, AND TISSUE SPECIFICITY.
RC   TISSUE=Gizzard;
RX   PubMed=7982954; DOI=10.1016/s0021-9258(18)43828-8;
RA   Shimizu H., Ito M., Miyahara M., Ichikawa K., Okubo S., Konishi T.,
RA   Naka M., Tanaka T., Hirano K., Hartshorne D.J., Nakano T.;
RT   "Characterization of the myosin-binding subunit of smooth muscle myosin
RT   phosphatase.";
RL   J. Biol. Chem. 269:30407-30411(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 681-1004, AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Gizzard;
RX   PubMed=7988720; DOI=10.1016/0014-5793(94)01231-8;
RA   Chen Y.H., Chen M.X., Alessi D.R., Campbell D.G., Shanahan C., Cohen P.,
RA   Cohen P.T.W.;
RT   "Molecular cloning of cDNA encoding the 110 kDa and 21 kDa regulatory
RT   subunits of smooth muscle protein phosphatase 1M.";
RL   FEBS Lett. 356:51-55(1994).
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   PHOSPHORYLATION AT THR-695 AND THR-850.
RX   PubMed=12220642; DOI=10.1016/s0014-5793(02)03175-7;
RA   Velasco G., Armstrong C., Morrice N., Frame S., Cohen P.;
RT   "Phosphorylation of the regulatory subunit of smooth muscle protein
RT   phosphatase 1M at Thr850 induces its dissociation from myosin.";
RL   FEBS Lett. 527:101-104(2002).
RN   [4]
RP   PHOSPHORYLATION AT THR-695 AND THR-850, AND MUTAGENESIS OF THR-695 AND
RP   THR-850.
RX   PubMed=10601309; DOI=10.1074/jbc.274.52.37385;
RA   Feng J., Ito M., Ichikawa K., Isaka N., Nishikawa M., Hartshorne D.J.,
RA   Nakano T.;
RT   "Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle
RT   myosin phosphatase.";
RL   J. Biol. Chem. 274:37385-37390(1999).
RN   [5]
RP   PHOSPHORYLATION BY DMPK.
RX   PubMed=11287000; DOI=10.1016/s0014-5793(01)02283-9;
RA   Muranyi A., Zhang R., Liu F., Hirano K., Ito M., Epstein H.F.,
RA   Hartshorne D.J.;
RT   "Myotonic dystrophy protein kinase phosphorylates the myosin phosphatase
RT   targeting subunit and inhibits myosin phosphatase activity.";
RL   FEBS Lett. 493:80-84(2001).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-299 IN COMPLEX WITH PPP1CB.
RX   PubMed=15164081; DOI=10.1038/nature02582;
RA   Terrak M., Kerff F., Langsetmo K., Tao T., Dominguez R.;
RT   "Structural basis of protein phosphatase 1 regulation.";
RL   Nature 429:780-784(2004).
CC   -!- FUNCTION: Regulates myosin phosphatase activity.
CC       {ECO:0000269|PubMed:7982954}.
CC   -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC,
CC       and one or several targeting or regulatory subunits (By similarity).
CC       PPP1R12A mediates binding to myosin. {ECO:0000250,
CC       ECO:0000269|PubMed:15164081, ECO:0000269|PubMed:7982954}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14974}.
CC       Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:O14974}.
CC       Note=Also along actomyosin filaments. {ECO:0000250|UniProtKB:O14974}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=M133;
CC         IsoId=Q90623-1; Sequence=Displayed;
CC       Name=2; Synonyms=M130;
CC         IsoId=Q90623-2; Sequence=VSP_035912;
CC   -!- TISSUE SPECIFICITY: Detected in brain, lung, aorta, heart, gizzard,
CC       stomach, oviduct, spleen, kidney and small intestine.
CC       {ECO:0000269|PubMed:7982954}.
CC   -!- PTM: Phosphorylated by CIT (Rho-associated kinase) and by ROCK2 on
CC       serine and threonine residues. Phosphorylation at Thr-695 leads to
CC       inhibition of myosin phosphatase activity. Phosphorylation at Thr-850
CC       abolishes myosin binding. May be phosphorylated at Thr-695 by DMPK; may
CC       inhibit the myosin phosphatase activity. {ECO:0000269|PubMed:10601309,
CC       ECO:0000269|PubMed:11287000, ECO:0000269|PubMed:12220642}.
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DR   EMBL; D37985; BAA07201.1; -; mRNA.
DR   EMBL; D37986; BAA07202.1; -; mRNA.
DR   EMBL; S74623; AAB32730.1; -; mRNA.
DR   PIR; A55142; A55142.
DR   RefSeq; NP_990454.1; NM_205123.1. [Q90623-1]
DR   RefSeq; XP_015133641.1; XM_015278155.1.
DR   RefSeq; XP_015133841.1; XM_015278355.1. [Q90623-2]
DR   PDB; 1S70; X-ray; 2.70 A; B=1-299.
DR   PDBsum; 1S70; -.
DR   AlphaFoldDB; Q90623; -.
DR   BMRB; Q90623; -.
DR   SMR; Q90623; -.
DR   BioGRID; 676290; 1.
DR   ELM; Q90623; -.
DR   IntAct; Q90623; 1.
DR   STRING; 9031.ENSGALP00000016789; -.
DR   iPTMnet; Q90623; -.
DR   PaxDb; Q90623; -.
DR   PRIDE; Q90623; -.
DR   Ensembl; ENSGALT00000065339; ENSGALP00000055263; ENSGALG00000010325. [Q90623-1]
DR   Ensembl; ENSGALT00000090229; ENSGALP00000062528; ENSGALG00000010325. [Q90623-2]
DR   GeneID; 396020; -.
DR   KEGG; gga:396020; -.
DR   CTD; 4659; -.
DR   VEuPathDB; HostDB:geneid_396020; -.
DR   eggNOG; KOG0505; Eukaryota.
DR   GeneTree; ENSGT00940000156120; -.
DR   InParanoid; Q90623; -.
DR   OrthoDB; 477969at2759; -.
DR   PhylomeDB; Q90623; -.
DR   BRENDA; 3.1.3.53; 1306.
DR   Reactome; R-GGA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-GGA-5627123; RHO GTPases activate PAKs.
DR   EvolutionaryTrace; Q90623; -.
DR   PRO; PR:Q90623; -.
DR   Proteomes; UP000000539; Chromosome 1.
DR   Bgee; ENSGALG00000010325; Expressed in colon and 13 other tissues.
DR   ExpressionAtlas; Q90623; baseline and differential.
DR   GO; GO:0031672; C:A band; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
DR   GO; GO:0030018; C:Z disc; ISS:UniProtKB.
DR   GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
DR   GO; GO:0004857; F:enzyme inhibitor activity; IBA:GO_Central.
DR   GO; GO:0019208; F:phosphatase regulator activity; ISS:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR   GO; GO:0035508; P:positive regulation of myosin-light-chain-phosphatase activity; IBA:GO_Central.
DR   GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB.
DR   GO; GO:0035507; P:regulation of myosin-light-chain-phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   DisProt; DP00218; -.
DR   Gene3D; 1.25.40.20; -; 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR017401; MYPT1/MYPT2/Mbs85.
DR   InterPro; IPR031775; PRKG1_interact.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF15898; PRKG1_interact; 1.
DR   PIRSF; PIRSF038141; PP1_12ABC_vert; 1.
DR   SMART; SM00248; ANK; 6.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ANK repeat; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..1004
FT                   /note="Protein phosphatase 1 regulatory subunit 12A"
FT                   /id="PRO_0000355556"
FT   REPEAT          39..68
FT                   /note="ANK 1"
FT   REPEAT          72..101
FT                   /note="ANK 2"
FT   REPEAT          105..134
FT                   /note="ANK 3"
FT   REPEAT          138..164
FT                   /note="ANK 4"
FT   REPEAT          198..227
FT                   /note="ANK 5"
FT   REPEAT          231..260
FT                   /note="ANK 6"
FT   REGION          35..38
FT                   /note="Important for interaction with PPP1CB"
FT   REGION          291..920
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..331
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..355
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..413
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..431
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        539..613
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        637..658
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        659..685
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        707..765
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        766..811
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        812..839
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        859..883
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        884..911
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         695
FT                   /note="Phosphothreonine; by ROCK2"
FT                   /evidence="ECO:0000269|PubMed:10601309,
FT                   ECO:0000269|PubMed:12220642"
FT   MOD_RES         850
FT                   /note="Phosphothreonine; by ROCK2"
FT                   /evidence="ECO:0000269|PubMed:10601309,
FT                   ECO:0000269|PubMed:12220642"
FT   VAR_SEQ         512..552
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:7982954"
FT                   /id="VSP_035912"
FT   MUTAGEN         695
FT                   /note="T->A: Reduces phosphorylation. Reduces
FT                   phosphorylation on serine and threonine residues by 80%;
FT                   when associated with A-850."
FT                   /evidence="ECO:0000269|PubMed:10601309"
FT   MUTAGEN         850
FT                   /note="T->A: Reduces phosphorylation. Reduces
FT                   phosphorylation on serine and threonine residues by 80%;
FT                   when associated with A-695."
FT                   /evidence="ECO:0000269|PubMed:10601309"
FT   HELIX           4..19
FT                   /evidence="ECO:0007829|PDB:1S70"
FT   TURN            20..22
FT                   /evidence="ECO:0007829|PDB:1S70"
FT   HELIX           40..50
FT                   /evidence="ECO:0007829|PDB:1S70"
FT   HELIX           53..62
FT                   /evidence="ECO:0007829|PDB:1S70"
FT   HELIX           76..82
FT                   /evidence="ECO:0007829|PDB:1S70"
FT   HELIX           86..94
FT                   /evidence="ECO:0007829|PDB:1S70"
FT   HELIX           109..116
FT                   /evidence="ECO:0007829|PDB:1S70"
FT   HELIX           119..127
FT                   /evidence="ECO:0007829|PDB:1S70"
FT   HELIX           142..145
FT                   /evidence="ECO:0007829|PDB:1S70"
FT   HELIX           149..162
FT                   /evidence="ECO:0007829|PDB:1S70"
FT   HELIX           166..187
FT                   /evidence="ECO:0007829|PDB:1S70"
FT   TURN            196..198
FT                   /evidence="ECO:0007829|PDB:1S70"
FT   HELIX           202..209
FT                   /evidence="ECO:0007829|PDB:1S70"
FT   HELIX           212..219
FT                   /evidence="ECO:0007829|PDB:1S70"
FT   TURN            220..222
FT                   /evidence="ECO:0007829|PDB:1S70"
FT   HELIX           235..241
FT                   /evidence="ECO:0007829|PDB:1S70"
FT   HELIX           245..253
FT                   /evidence="ECO:0007829|PDB:1S70"
FT   TURN            268..270
FT                   /evidence="ECO:0007829|PDB:1S70"
FT   HELIX           275..277
FT                   /evidence="ECO:0007829|PDB:1S70"
FT   HELIX           278..286
FT                   /evidence="ECO:0007829|PDB:1S70"
SQ   SEQUENCE   1004 AA;  111606 MW;  7ED870DB87046929 CRC64;
     MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RKKTKVKFDD GAVFLAACSS GDTEEVLRLL
     ERGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN QPDNEGWIPL HAAASCGYLD
     IAEYLISQGA HVGAVNSEGD TPLDIAEEEA MEELLQNEVN RQGVDIEAAR KEEERIMLRD
     ARQWLNSGHI NDVRHAKSGG TALHVAAAKG YTEVLKLLIQ ARYDVNIKDY DGWTPLHAAA
     HWGKEEACRI LVENLCDMEA VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKREKKSP
     LIESTANLDN NQTQKTFKNK ETLIMEQEKN ASSIESLEHE KADEEEEGKK DESSCSSEEE
     EDDDSESEAE TDKAKTLANA NTTSTQSASM TAPSVAGGQG TPTSPLKKFP TSTTKVSPKE
     EERKDESPAS WRLGLRKTGS YGALAEITAS KEAQKEKDSA GVIRSASSPR LSSSLDNKEK
     EKDGKGTRLA YVAPTIPRRL ASTSDIDEKE NRDSSASSIR SGSSYARRKW EEDVKKNSLN
     EGPTSLNTSY QRSGSFGRRQ DDLVSSNVPS TASTVTSSAG LQKTLPASAN TTTKSTTGST
     SAGVQSSTSN RLWAEDSTEK EKDSVPTAVT VPVAPSVVNA AATTTAMTTA TSGTVSSTSE
     VRERRRSYLT PVRDEESESQ RKARSRQARQ SRRSTQGVTL TDLQEAEKTI GRSRSTRTRE
     QENEEKEKEE KEKQDKEKQE EKKESETKDD DYRQRYSRTV EEPYHRYRPT STSTSTSSTS
     SLSTSTSSLS SSSQLNRPNS LIGITSAYSR SGTKESEREG GKKEEEKEED KSQPKSIRER
     RRPREKRRST GVSFWTQDSD ENEQEHQSDS EEGTNKKETQ SDSLSRYDTG SLSVSSGDRY
     DSAQGRSGSQ SYLEDRKPYC SRLEKEDSTD FKKLYEQILA ENEKLKAQLH DTNMELTDLK
     LQLEKTTQRQ ERFADRSLLE MEKRVSGKSQ YLLGGKKSSR KKDI
 
 
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