ID A0A096NJ57_PAPAN Unreviewed; 1388 AA.
AC A0A096NJ57;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Rho-associated protein kinase {ECO:0000256|PIRNR:PIRNR037568};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR037568};
GN Name=ROCK2 {ECO:0000313|Ensembl:ENSPANP00000013006.3};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000013006.3, ECO:0000313|Proteomes:UP000028761};
RN [1] {ECO:0000313|Ensembl:ENSPANP00000013006.3, ECO:0000313|Proteomes:UP000028761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPANP00000013006.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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|ARBA:ARBA00001433,
CC 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|ARBA:ARBA00000775,
CC 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: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000256|ARBA:ARBA00004300}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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 RefSeq; XP_003908333.1; XM_003908284.3.
DR Ensembl; ENSPANT00000019515.3; ENSPANP00000013006.3; ENSPANG00000016385.4.
DR GeneID; 101003099; -.
DR KEGG; panu:101003099; -.
DR CTD; 9475; -.
DR GeneTree; ENSGT01030000234517; -.
DR OMA; NSQWIVQ; -.
DR Proteomes; UP000028761; Chromosome 14.
DR Bgee; ENSPANG00000016385; Expressed in skeletal muscle tissue and 68 other cell types or tissues.
DR ExpressionAtlas; A0A096NJ57; baseline.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0072518; F:Rho-dependent protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0007249; P:canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0071394; P:cellular response to testosterone stimulus; IEA:Ensembl.
DR GO; GO:0051298; P:centrosome duplication; IEA:Ensembl.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0044788; P:modulation by host of viral process; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:1903347; P:negative regulation of bicellular tight junction assembly; IEA:Ensembl.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IEA:Ensembl.
DR GO; GO:0150033; P:negative regulation of protein localization to lysosome; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; IEA:Ensembl.
DR GO; GO:0010825; P:positive regulation of centrosome duplication; IEA:InterPro.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:1903140; P:regulation of establishment of endothelial barrier; IEA:Ensembl.
DR GO; GO:0045616; P:regulation of keratinocyte differentiation; IEA:Ensembl.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:UniProtKB-UniRule.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0006939; P:smooth muscle contraction; IEA:InterPro.
DR CDD; cd20875; C1_ROCK2; 1.
DR CDD; cd11638; HR1_ROCK2; 1.
DR CDD; cd01242; PH_ROCK; 1.
DR CDD; cd22250; ROCK_SBD; 1.
DR CDD; cd05621; STKc_ROCK2; 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; IPR029878; ROCK2_cat.
DR InterPro; IPR037311; ROCK2_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:SF28; RHO-ASSOCIATED PROTEIN KINASE 2; 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; 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 Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01207}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000028761};
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 92..354
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 357..425
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 497..573
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 979..1047
FT /note="RhoBD"
FT /evidence="ECO:0000259|PROSITE:PS51859"
FT DOMAIN 1150..1349
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1260..1315
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1345..1388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 449..1009
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1056..1101
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1363..1388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 214
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037568-1"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR037568-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1388 AA; 160866 MW; FFE1438FDF5BB109 CRC64;
MSRPPPTGKM PGAPETVPGD GAGASRQRKL EALIRDPRSP INVESLLDGL NSLVLDLDFP
ALRKNKNIDN FLNRYEKIVK KIRGLQMKAE DYDVVKVIGR GAFGEVQLVR HKASQKVYAM
KLLSKFEMIK RSDSAFFWEE RDIMAFANSP WVVQLFYAFQ DDRYLYMVME YMPGGDLVNL
MSNYDVPEKW AKFYTAEVVL ALDAIHSMGL IHRDVKPDNM LLDKHGHLKL ADFGTCMKMD
ETGMVHCDTA VGTPDYISPE VLKSQGGDGY YGRECDWWSV GVFLFEMLVG DTPFYADSLV
GTYSKIMDHK NSLCFPEDAE ISKHAKNLIC AFLTDREVRL GRNGVEEIRQ HPFFKNDQWH
WDNIRETAAP VVPELSSDID SSNFDDIEDD KGDVETFPIP KAFVGNQLPF IGFTYYRENL
LLSDSPSCRE NDSIQSRKNE ESQEIQKKLY TLEEHLSSEI QAKEELEQKC KSVNTRLEKT
AKELEEEITL RKSVESALRQ LEREKALLQH KNAEYQRKAD HEADKKRNLE NDVNSLKDQL
EDLKKRNQNS QISTEKVNQL QRQLDETNAL LRTESDTAAR LRKTQAETSK QIQQLESNNR
DLQDKNCLLE TAKLKLEKEF INLQSALESE RRDRTHGSEI INDLQGRISG LEEDLKNGKI
LIAKVELEKR QLQERFTDLE KEKSNMEIDM TYQLKVIQQS LEQEEAEHKA TKARLADKNK
IYESIEEAKS EAMKEMEKKL LEERTLKQKV ENLLLEAEKR CSILDCDLKQ SQQKINELLK
QKDVLNEDVR NLTLKIEQET QKRCLTQNDL KMQTQQVNTL KMSEKQLKQE NNHLMEMKMN
LEKQNAELRK ERQDADGQMK ELQDQLEAEQ YFSTLYKTQV RELKEECEEK TKLGKELQQK
KQELQDERDS LAAQLEITLT KADSEQLARS IAEEQYSDLE KEKIMKELEI KEMMARHKQE
LTEKDATIAS LEETNRTLTS DVANLANEKE ELNNKLKDVQ EQLSRLKDEE ISAAAIKAQF
EKQLLTERTL KTQAVNKLAE IMNRKEPVKR GNDTDVRRKE KENRKLHMEL KSEREKLTQQ
MIKYQKELNE MQAQIAEESQ IRIELQMTLD SKDSDIEQLR SQLQALHIGL DSSSIGSGPG
DAEADDGFPE SRLEGWLSLP ARNNTKKFGW VKKYVIVSSK KILFYDSEQD KEQSNPYMVL
DIDKLFHVRP VTQTDVYRAD AKEIPRIFQI LYANEGESKK EQEFPVEPVG EKSNYICHKG
HEFIPTLYHF PTNCEACMKP LWHMFKPPPA LECRRCHIKC HKDHMDKKEE IIAPCKVYYD
ISTAKNLLLL ANSTEEQQKW VSRLVKKIPK KPPAPDPFAR SSPRTSMKIQ QNQSIRRPSR
QLAPNKPS
//
