ID A0A2K6RBN2_RHIRO Unreviewed; 1763 AA.
AC A0A2K6RBN2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Alpha kinase 3 {ECO:0000313|Ensembl:ENSRROP00000038452.1};
GN Name=ALPK3 {ECO:0000313|Ensembl:ENSRROP00000038452.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000038452.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000038452.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Alpha-type
CC protein kinase family. ALPK subfamily. {ECO:0000256|ARBA:ARBA00008651}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 61622.ENSRROP00000038452; -.
DR Ensembl; ENSRROT00000062926.1; ENSRROP00000038452.1; ENSRROG00000042611.1.
DR GeneTree; ENSGT00940000158534; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0055013; P:cardiac muscle cell development; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.20.200.10; MHCK/EF2 kinase; 1.
DR InterPro; IPR004166; a-kinase_dom.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR47091; ALPHA-PROTEIN KINASE 2-RELATED; 1.
DR PANTHER; PTHR47091:SF1; ALPHA-PROTEIN KINASE 3; 1.
DR Pfam; PF02816; Alpha_kinase; 1.
DR Pfam; PF07679; I-set; 1.
DR SMART; SM00811; Alpha_kinase; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 3: Inferred from homology;
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 149..240
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1339..1427
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1455..1683
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 56..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1688..1763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1701..1735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1763 AA; 187051 MW; 6C1836CCEDE4F33F CRC64;
MQVAGFVYVL GQQPLARQGE GQSGLVPGRG PVLWLPGLLR SSSSWPCGPL ICKTGHKQGR
KASRESGPGS STKGPVLVSM FTLLPVGRSG AGGDGEDDGP VWIPSPASRS YLLSVRPETS
LSSNRLSHPS SGRSTFCSII AQLTEETQPL FETTLKSRAV SEDSDVRFTC IVTGYPEPEV
TWYKDDMELD RYCGLPKYEI THQGNRHTLQ LYRCREEDAA IYQASAQNSK GIVSCSGVLE
VGTMTEYKIH QRWFAKLKRK AAAKLREIEQ SWKHEKAAPG EADTLRKLSP DRFQRKRRLS
GAEALDPSVP TRDPEGGTLA VWQEGETESA QHSGLGLINS FASGEVTTNG EAAPENGEDG
GEHGLLTYIC DAMELGPQRV LKEESGAKKK KKDEESKQGL RKPELEKAAP SRLSSENCIP
NSDEPDSCGT QGPAGMEQVQ TQPRGRAARG PGSSGTDSTR KPTSAVGTPD KAQKAPAPGQ
EVYFSLKDMY LENTGAVRLL GEDCPQTLSV QAPGESLKGK APIRARDEGV PGAPGQPTHS
FTPQPTRPFN RKRFAPPKPK GEATPDSKPI SSLSQAPECG AQSLMKAPPQ ASVQVPTPPA
RRRHGTRDSP LQGQAGHRTP GEVLECQTTM APTVSASSSS GVASIGCSTS GSQGIFESID
METQEDGRTS ANQRTGSKKN VQADGKIQVD GRTRGDGTQT AQRTQADRKT QVDAGTQESK
RPQSERSAQK VMVTQGRAET QLETTQAGEK VQEDRKAQAD EGTQEDRRMQ EEKRMQSAGS
APTATEGQSE QEAVTSLGPP SRTPELPPTE GPRAPLSIEC FTQIPEGSCV PEKPGFPPRS
EEAAVTASRN HEQTVLGPLS GNLMLPAQPP HEGSVEQVGG ERCQGPQSSG PVQAKQEDSP
FQYPKEEQPG GVLCVDQGGC PPAGLSQEVP TMPSLPGTEL TASPKEGPSS TLTSQHRSTA
AFLPSEDQAL ISSAPTLHLG PGTPTQSHPP ETMATSSEGA YAQVSDVEGR TPGPRSCDPG
LIDSLKNYLL LLLKLSSTET SGAGGESQVG AATGGLAPSA TLTPTVEVAG LSPRTSRRIL
ERVENNHLVQ SAQTLLLSPC TSRRLTGLLD HEVQAGRQAL AAARGSWGPG PSSLTVPAIV
VDEEGPGLAS EGASEGEGEV SLEGPGLLGA SQESSMGDRL GEAGRQAVPG QGPSTESIAQ
EPSQEEKFPG EALTGLPAAT PEELALGARR KRFLPKVRAA GDGEATTPEE RESPTVSPRG
PRKSLVPGSP GTPGRERRSP TQGRKASMLE VPRAEEELAA GDLSPSPKAG GLNTELALDE
GKQETLAKPR KAKDLLKAPQ VIRKIRVEQF PDASGSLKLW CQFFNILSDS VLTWAKDQCP
VGEVGRSAGD EGPAALAIVQ ASPVDCGVYR CTIHNEHGSA STDFCLSPEV LSGFISREEG
EVGEEIEMTP MVFAKGLADS GCWGDKLFGR LVSEELRGGG YGCVLRKASQ AKVIYGLEPI
FESGRTCIIK VSSLLVFGPS SETSLVGRNY DVTIQVLCPR IQNWVGGRSS LGHTSCLLII
PLYLIYRPAN NIPYATLEED LGKPLESYCS REWGCAGAVT ASSSSEAMQK CQTFQHWLYQ
WTNGSFLVTD LAGVDWKMTD VQIATKLRGY QGLKESCFPA LLDQFASSHQ CNAYCELLGL
THLKGPEVAH PQAKAKGSKS PSAGRKSSQL SPQPQKKGLP SPQGTRKSAA SSKAAPQASG
PVAAQLLGQP PTQEEGSKAQ GMR
//