ID A0A3B5QR17_XIPMA Unreviewed; 1423 AA.
AC A0A3B5QR17;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=ROCK2 {ECO:0000313|Ensembl:ENSXMAP00000033036.1};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000033036.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000033036.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000033036.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {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}.
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DR Ensembl; ENSXMAT00000030024.1; ENSXMAP00000033036.1; ENSXMAG00000017805.2.
DR GeneTree; ENSGT01030000234517; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:UniProtKB-UniRule.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd20875; C1_ROCK2; 1.
DR CDD; cd01242; PH_ROCK; 1.
DR CDD; cd22250; ROCK_SBD; 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; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR020684; ROCK1/ROCK2.
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; PF00433; Pkinase_C; 1.
DR Pfam; PF08912; Rho_Binding; 1.
DR PIRSF; PIRSF037568; Rho_kinase; 1.
DR SMART; SM00109; C1; 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 SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 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};
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
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 Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 3..288
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 289..359
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 435..511
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 917..985
FT /note="RhoBD"
FT /evidence="ECO:0000259|PROSITE:PS51859"
FT DOMAIN 1274..1329
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 356..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1363..1423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 892..964
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 991..1020
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 365..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1409..1423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 148
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037568-1"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR037568-2"
SQ SEQUENCE 1423 AA; 164442 MW; 70C7BC8D26955F88 CRC64;
MSESLLLSHQ NGDLPTVFSL LSLCSCYSLH HHLSLSDWPY LQVRHKASKK VYAMKQLSKF
EMIKRSDSAF FWEERHIMAF SNSPWIVQLC CAFQDDRNLY MVMEFMPGGD MVTLTINYDI
PEKWARFYTA ELVLALDAIH SMGFIHRDIK PDNMLLDQHG HLKLADFGTC MRMNSSGMVH
CETAVGTPDY ISPEVLQSQG GDGTYGRECD WWSVGVSLYE LLVGETPFYA ESLIGTYGKI
MNHHNALVFP DDVEMSQNAK DLISAFLTDR KVRLGRTGVD EIKRHPFFKD DQWTFDNIRD
TVAPVVPELN SDIDTSNFDE IEVEKGTAET FPPPRAFAGN QLPFIGFTYF KEDQLLSGSG
SSPEEDSDNC KDTENSADSK KDLQKKVKQL EEQLDHEMQA KDELEQKCRN ATNRLDKLVN
ELDKEMNSRQ KVEASMRQLE RERALLQHQS VENQRKVEME ADRKRILENE LNNLRDQLED
QKKRNQHSQI SNEKNIQLQK QLNEANDALQ AEQEAVTRLK RSQAETQKQA QSLEVSLREM
EKKCSGLEAS KAEQEKQMRG LQVELEEERG EHNLRTETLA DLQGTISLLE DEVKEVKSSL
SKVNSEKKEL QTKLNNLEKE KNNQAIDLAF QLKSLQQSLE QEEAEHKATK AKLADKSEIY
KSIEEAKSEA LKGMESTLQE ERNLKLQVEE QLLQLKKEHS MLDCDHKQAE QKLEELQAQK
EKLSEEVMDL TLRLEQETRK RSLSQSDLKA QKQQVSALAS SEKQLKQELN QLLDMKQSLE
KQNQKLHREK QEADGQLKEL KDQLEAEQYF TTLYKTQIRE LKDECNEKNK MYKEAQQQLA
EYQEERDSLA AQLESSLTKA DSEQLARSIA EEQYSLLEKE KIMKELEIKD MMARHKQELS
EKEATIGSLE ESNRTLTVDV ANLASEKEEL NNQLKDLQQE LQKAKELKKE LESLKVSFER
QVQTERTLKI QAVNKLAEVM NQKKEKGRGG VRAVDSEVHK KEKENRKLQL ELKAERQNLN
SIIFKYQKEL DDMQAMMVEE THMRQELQMA LDSKDSDIER LRCQITSLSV HSLDSTSISS
NNDLEMADGF PVSITHSRTS ESMSFTYQRT HKSVRVDTRP NLHSARALFD SESEDEEEDE
EPKEHCQRPL ALTYLQSREP EAGDSRLEDW ISLPSKNTKR FGWDKKYVVV SSKKILFYNS
QMDQEQANPF MTLDIEKLFH VRPITQTDCY RADVKEIPRI FQILYANEGE SKRDQEAVEE
PAPCERSNYI MHKGHEFINT LYHLPCSCEV CVRPLWNVFK PPAALECRCC HTKYHKDHLD
KKEDNIPPCK VNYDMSTAKE LLLLTSSQTE QQRWVNHLLK RIPKKNPTLS PPPAARNSPI
ESLPFSSPHM SPESSPKDSP RLSHRRAIKI PSTRQQQTSD KSS
//
