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Database: UniProt
Entry: L8ICB7_9CETA
LinkDB: L8ICB7_9CETA
Original site: L8ICB7_9CETA 
ID   L8ICB7_9CETA            Unreviewed;      1354 AA.
AC   L8ICB7;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=Rho-associated protein kinase {ECO:0000256|PIRNR:PIRNR037568};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR037568};
GN   ORFNames=M91_00549 {ECO:0000313|EMBL:ELR54145.1};
OS   Bos mutus (wild yak).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=72004 {ECO:0000313|EMBL:ELR54145.1, ECO:0000313|Proteomes:UP000011080};
RN   [1] {ECO:0000313|EMBL:ELR54145.1, ECO:0000313|Proteomes:UP000011080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=yakQH1 {ECO:0000313|Proteomes:UP000011080};
RX   PubMed=22751099; DOI=10.1038/ng.2343;
RA   Qiu Q., Zhang G., Ma T., Qian W., Wang J., Ye Z., Cao C., Hu Q., Kim J.,
RA   Larkin D.M., Auvil L., Capitanu B., Ma J., Lewin H.A., Qian X., Lang Y.,
RA   Zhou R., Wang L., Wang K., Xia J., Liao S., Pan S., Lu X., Hou H., Wang Y.,
RA   Zang X., Yin Y., Ma H., Zhang J., Wang Z., Zhang Y., Zhang D., Yonezawa T.,
RA   Hasegawa M., Zhong Y., Liu W., Zhang Y., Huang Z., Zhang S., Long R.,
RA   Yang H., Wang J., Lenstra J.A., Cooper D.N., Wu Y., Wang J., Shi P.,
RA   Wang J., Liu J.;
RT   "The yak genome and adaptation to life at high altitude.";
RL   Nat. Genet. 44:946-949(2012).
CC   -!- FUNCTION: Protein kinase which is a key regulator of actin cytoskeleton
CC       and cell polarity. {ECO:0000256|PIRNR:PIRNR037568}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|PIRNR:PIRNR037568};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|PIRNR:PIRNR037568};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|PIRNR:PIRNR037568};
CC   -!- ACTIVITY REGULATION: Activated by RHOA binding. Inhibited by Y-27632.
CC       {ECO:0000256|PIRNR:PIRNR037568}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR037568}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. {ECO:0000256|ARBA:ARBA00009903,
CC       ECO:0000256|PIRNR:PIRNR037568}.
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DR   EMBL; JH881470; ELR54145.1; -; Genomic_DNA.
DR   STRING; 72004.ENSBMUP00000029495; -.
DR   Proteomes; UP000011080; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007266; P:Rho protein signal transduction; IEA:UniProtKB-UniRule.
DR   CDD; cd20874; C1_ROCK1; 1.
DR   CDD; cd11639; HR1_ROCK1; 1.
DR   CDD; cd01242; PH_ROCK; 1.
DR   CDD; cd22250; ROCK_SBD; 1.
DR   CDD; cd05622; STKc_ROCK1; 1.
DR   Gene3D; 1.20.5.340; -; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.20.5.730; Single helix bin; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR011072; HR1_rho-bd.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR020684; ROCK1/ROCK2.
DR   InterPro; IPR037310; ROCK1_HR1.
DR   InterPro; IPR015008; ROCK_Rho-bd_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR   PANTHER; PTHR22988:SF73; RHO-ASSOCIATED PROTEIN KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08912; Rho_Binding; 1.
DR   PIRSF; PIRSF037568; Rho_kinase; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF103652; G protein-binding domain; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS51860; REM_1; 1.
DR   PROSITE; PS51859; RHO_BD; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR037568};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW   ProRule:PRU01207};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00023212, ECO:0000256|PIRNR:PIRNR037568};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW   ECO:0000256|PIRNR:PIRNR037568};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR037568};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR037568};
KW   Membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR037568};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR037568};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011080};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|PIRNR:PIRNR037568};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037568};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          76..338
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          341..409
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   DOMAIN          479..556
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          949..1015
FT                   /note="RhoBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51859"
FT   DOMAIN          1118..1317
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1228..1283
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   REGION          1319..1354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          432..898
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          938..979
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1020..1100
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1326..1354
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        198
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037568-1"
FT   BINDING         105
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037568-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1354 AA;  158370 MW;  9E1F16F064F6AD72 CRC64;
     MSTGDSFETR FEKIDNLLRD PKSEVNSDCL LDGLDALVYD LDFPALRKNK NIDNFLSRYK
     DTINKIRDLR MKAEDYEVVK VIGRGAFGEV QLVRHKSTRK VYAMKLLSKF EMIKRSDSAF
     FWEERDIMAF ANSPWVVQLF YAFQDDRYLY MVMEYMPGGD LVNLMSNYDV PEKWARFYTA
     EVVLALDAIH SMGFIHRDVK PDNMLLDKSG HLKLADFGTC MKMNKEGMVR CDTAVGTPDY
     ISPEVLKSQG GDGYYGRECD WWSVGVFLYE MLVGDTPFYA DSLVGTYSKI MNHKNSLTFP
     DDNDISKEAK NLICAFLTDR EVRLGRNGVE EIKRHLFFKN DQWAWETLRD TVAPVVPDLS
     SDIDTSNFDD LEEDKGDEET FPIPKAFVGN QLPFVGFTYY SNRRYLSSAN PNDNRTSSNV
     DKSLQENLQK TIYKLEEQLH NEMQLKDEME QKCRTSNIKL DKIMKELDEE GNQRRNLEST
     VSQIEKEKML LQHRINEYQR KAEQENEKRR NVENEVSTLK DQLEDLKKVS QNSQLANEKL
     AQLQKQLEEA NDLLRTESDT AVRLRKSHTE MSKSITQLES LNRELQERNR ILENSKSQMD
     KDYYQLQAVL EAERRDRGHD SEKIGDLQAR ITSLQEEVKH LKHNLERVEG ERKEAQDMLN
     HSEKEKNNLE IDLNYKLKSL QQRLEQEVNE HKVTKARLTD KHQSIEEAKS VAMCEMEKKL
     KEERDAREKA ENRVVQIEKQ CSMLDVDLKQ SQQKLEHLIE NKDRMEDEVK NLTLQLEQES
     NKRLLLQNEL KTQAFEADNL KGLEKQMKQE INTLLEAKRL LEFELAQLTK QYRGNEGQMR
     ELQDQLEAEQ YFSTLYKTQV KELKEEIEEK NRENLKKIQE LQSEKETLAT QLDLAETKAE
     SEQLARGLLE EQYFELTQES KKAASRNRQE ITDKDHTLSR LEETNSMLTK DIELLRKENE
     ELTDKMRKAE EEYKLKKEEE INILKAAFEK NINTERTLKT QAVNKLAEIM NRKDFKIDRK
     KANTQDLRKK EKENRKLQLE LNQEREKFNQ MVVKHQKELN EMQAQLVEEC THKNELQMQL
     ASKESDIEQL RAKLLDLSDS TSVASFPSAD ETDGNLPESR IEGWLSIPNR GNIKRYGWKK
     QYVVVSSKKI LFYNDEQDKE QSNPSMVLDI DKLFHVRPVT QGDVYRAETE EIPKIFQILY
     ANEGECRKDL EVEPVQQAEK TNFQNHKGHE FIPTLYHFPA NCEACAKPLW HVFKPPPALE
     CRRCHVKCHR DHIDKKEDLI SPCKVSYDVT SARDMLLLAC SQDEQKKWVT HLVKKIPKNP
     PSGFVRASPR TLSTRSTANQ SFRKVVKNTS GKAR
//
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