ID G1SQ37_RABIT Unreviewed; 1548 AA.
AC G1SQ37;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Alpha kinase 3 {ECO:0000313|Ensembl:ENSOCUP00000005190.3};
GN Name=ALPK3 {ECO:0000313|Ensembl:ENSOCUP00000005190.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000005190.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000005190.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000005190.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000005190.3};
RG Ensembl;
RL Submitted (NOV-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 SMR; G1SQ37; -.
DR STRING; 9986.ENSOCUP00000005190; -.
DR PaxDb; 9986-ENSOCUP00000005190; -.
DR Ensembl; ENSOCUT00000005996.3; ENSOCUP00000005190.3; ENSOCUG00000005991.3.
DR eggNOG; ENOG502QPP5; Eukaryota.
DR GeneTree; ENSGT00940000158534; -.
DR HOGENOM; CLU_003270_0_0_1; -.
DR InParanoid; G1SQ37; -.
DR TreeFam; TF332629; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000005991; Expressed in skeletal muscle tissue and 15 other cell types or tissues.
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; 1.
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; 1.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 3: Inferred from homology;
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 51..147
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1291..1537
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 185..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1527..1548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..802
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1548 AA; 163468 MW; CB7C73FCAF32A0F0 CRC64;
MWSPGMAQGS RGWFCTVAPE LCLGSEFIWL FASPRSTFCS IIAQLTEETQ PLFETTLKSK
AVSEDSDVRF TCIVTGYPEP EVTWYKDDTE LDRYCGLPKY EITHQGNRHT LQLYRCREED
AAIYQASARN TKGIVSCSGV LEVGTMTEYK IHQRWFAKLK RKAAAKMREI EQSWKHGKEA
VGEADVLRKL SPDRFQRKRR LSGGQAPGPP APAREAEEGS RTWQEGDTES AQHPDLGLIT
SFAPEEMPTN GEAAPENGED GEHGLLTYIC EAMELRPHRA PKKESRAKKK KKEEESKQSV
RKPELEKAVG SHRSSESNTP SSNKPDARAT QGPTDVGQGH SQPRGRASRG PGPSRVDNTG
KPASAMGTND KAQDSSAPGP TQEVYFSLKD MYMESTRAAR PQGEEGSQTP SVRVSGENLS
GQLSIEAGGE RVPAAPGQSL PSLAPQPTRP VNRKRFAPPK PRAEPTADSK PVSPLSQTPE
HGAQSLGKAP AQGSAQVPTP PARRRHSTRD SPLQGRAVHR TPGEVPESQA TTTAATLAGG
SSGVTSIGGG GTSRSHDVIE PMDTDTQAGG PSSADQRAGG EQDQQLRGEM QVEGRPWADG
AQRSQRTQAE GEMQVEVVTQ ESARPQSVES SQRGVVTQAE RTQAGEKTQE GTQMREAKGT
QSGGSAAAAT TGQLEPPSVT SLSPPAAAPQ LPSPEGPRPP QITGGFAQTP AGSRVPEEPG
FLLRPEEAAV PAPETHKETL TLPAQPPPGG SLEQKGGERG FPCPTEAQPG GMLCVDLGGC
PAAGPSQEGP SVPSPPGMGP TSSPREGLPS TLTAQHRGTA AIQPSADQAL PSSAPTLHLG
PGPPSQGHPS ETLGASSEGA CAKTPPGEGG TSGPRSCDPG LIDSLKNYLL LLLKLSSAQT
SGAGAEAQEG TAAGGLAAPS TLAPTVEVAG LSPRTSRRIL ERVENDHLVQ SAQTLLLSPC
TSRRLTGLLD REVQAGQRAL AAAQGSRGPG PSPLTVPAIV VGEEEGTRLA SEGPSEGEGE
LSPEGPGGPL GQAASGQGLL SAGGGAQEPF QEDEVPGEAL TDLPAATPEE LALGARRKRF
LPKVRAAGDG EAAKPEERES PTVSPRGSRK SLAPGSPGTP GRERRSPTQG RRAAMLEVPR
AEEEPALGSG PKASGADTEL GPDEGRQESL AKPRKAQDQL KAPQVIRKIR VEQFPDASGS
LKLWCQFFNI LSDSVLTWAK DQRPVGEVVP GDEGPAALGH SCKPSPVDCG VYPMHYPERA
RSRPSTDFCL SPRGGGQQPR EIEMTPMVFA KGLADSGCWG DKLFGRLVSE ELRGHGRGCG
LRKASQAKVI YGLDPLFESG RTCIIKVSSL LVFGPSSETS LLGRNYDVTI QGCKIQNMSR
EYCKIFAAEA RAAPGFGEVP EIIPLYLIYR PANSIPYATL EEDLGKPLES YCSREWGCAG
PPAASGVSEA VQKCQAFQHW LYQWTNGSFL VTDLAGVDWK MTDVQIATKL RGYQGLKESC
CPALLDQFPQ RKGAPSSKAT LQASEAAAAQ LLGEPPAQEG GSKAQGMR
//