ID A0A2K6SHF2_SAIBB Unreviewed; 2166 AA.
AC A0A2K6SHF2;
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 2 {ECO:0000313|Ensembl:ENSSBOP00000006822.1};
GN Name=ALPK2 {ECO:0000313|Ensembl:ENSSBOP00000006822.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000006822.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000006822.1}
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}.
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DR RefSeq; XP_003926086.1; XM_003926037.2.
DR RefSeq; XP_010335068.1; XM_010336766.1.
DR STRING; 39432.ENSSBOP00000006815; -.
DR Ensembl; ENSSBOT00000023566.1; ENSSBOP00000006815.1; ENSSBOG00000020381.1.
DR Ensembl; ENSSBOT00000023574.1; ENSSBOP00000006822.1; ENSSBOG00000020381.1.
DR KEGG; sbq:101048508; -.
DR GeneTree; ENSGT00940000160524; -.
DR OrthoDB; 5321836at2759; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; 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:1905223; P:epicardium morphogenesis; IEA:Ensembl.
DR GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl.
DR GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
DR GO; GO:0003308; P:negative regulation of Wnt signaling pathway involved in heart development; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR CDD; cd16974; Alpha_kinase_ALPK2; 1.
DR CDD; cd20951; IgI_titin_I1-like; 1.
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:SF2; ALPHA-PROTEIN KINASE 2; 1.
DR PANTHER; PTHR47091; ALPHA-PROTEIN KINASE 2-RELATED; 1.
DR Pfam; PF02816; Alpha_kinase; 1.
DR Pfam; PF07679; I-set; 2.
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:UP000233220};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..114
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1782..1870
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1897..2129
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 109..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1223..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1407..1483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1499..1534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1690..1724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2132..2166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1459..1476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2132..2154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2166 AA; 236064 MW; 3E9DE1F954DBECC4 CRC64;
MTDSKGPQRR LLCFLSTLLS QKVPEKSDAV LRCIISGQPK PEVTWYKNGQ AMEKRGIASS
YEFFENQYIH VLHLSCCTRS DAAVYQISAK NSFGMICCSA SVEVECSSEN PQLSPNWEDG
RETGWKNETG TYEESANQID EKEHPYKEEE STSPGTPRSA DSSPSKSHHS HSVQSLANLD
IRVSGSENPL GVKGTRQTGE AYDSGNTEEI ADGLLFLNSS HIYEKQDGCC SKTVPSTASK
FTDGGLNKDG PQDVSLHSSQ QNPKVQKYIS LSLPLSEATA HVYPGGSALV NKQPSPQVSS
EDSDSDYELC PEITLTYTEE FSDDDLEYLE CSDVMTDYSN AVWQRNLLGT EHVFLLESDD
EEVEFSEHCL GGCEHFLSGM GCGPRVSGDA GPMVATAGFC GHHSQPQEVG VRSSRASKHG
PSSPQTGMTL SLGPYQDGMS SVTEQGRYKL PTAPEAAEND YPGIQGETRD SHQAREFTSD
NLLNMDESIR EAEMKPLSGE LENSGMSQCW ETGAEKRVGE KDLRSKRGSQ KPARGRRLGM
KENPKKPNAN LRESTTEDTL PLCYAKESAN HPLTQSDKRE TSHATAAATD WNSHADAGEC
AISTQAEQEA KTLQTSTYSL SKGGNTNCKG EGMHVNTLFE TSQVPGWRHY QQVQTQETVR
GKISCSQMPA CSEPAGEESP FIGTTTISFS NSGGVHKENA SLAQHLEVKH CTFGPQQEEK
QDRDGNAPDH FREDLKHELS ISEANDENTS PGVFSRHLPQ DSHIDFREPV AVSVASPEST
DTALTLENVC DGPTDRGFVC AMECFEAGDQ GTCHDTTDAL VGAPVDKYLP QEICSVDLGR
AAGQSEVSDL CSADDKTLEG LFQTQVSETS VSMCEGSKDS NSATSSLFIS TFTLNISHAA
SEGATGKSLA KMENSTCPLA STVQAGQEPP SPSNSGGLEE TQLLSSESNP LVQFKEGRDR
SPSPSAADTT DTPASRSSIV GFPSEKPTTL TANNECLRVT RETEDTSTVT IATKVHPAKY
LAVSIPEDKY ADGTKERFPC ASRENVSQFP SQVHLGHILS GATTKSTKEL LCTEPSVPGV
THRVLQLPEG ESFCSNSPLQ LDHLSGDKSQ TVDRADFRRH EENFQEIGSE MRQGLQQQSL
SPQRSLPEHD FQGSLPMTSA AQEEINLVPL AHSLASSREG AEQHSGGGTR VSVVAEAAVE
EDSQAPSNVP SLSNILLEQP KERIPRNWKA GNKLKLTTPQ ASTSEIWPPR QLENSESKAS
DGSPTVPDRA RAVPDSLKTD ALVPELAPSE TAARAHSPQG ADSALADSRE SRKGEEPAIS
AHWRNLSSWG FSQPRLLESS VDPVGEKDLC VTDSLSAASE TGGTENVNYV SQDQEEKRLK
MDHAAFFKKF LTCPKILESS VDPIDETGVV EDTRAGNPEP SESKPGAARE GSQSNAGNVR
HGVEIQPAMW RVPSPQGTIL SEKRISSSQE GSMKWEAEQS QADEAKVEVQ TTIWQVVHPS
RGGARTPSGC SIGQIQEGSD GSLREAAQRK KDKAELISST SRLSSCLAKM THAPLGVDAH
NSTDQIHDVL EKDLVEPRNR QYVFSVSKKR GTVENECGKP LPSAPDVSRL PCTSAPEENV
TDVSISHRME EPKIEVLHIG ENKPPSSSSS SAKTLAFISR EHESEKAPTL LQDPCQKGTL
GYVRKAREKS LEARAGKSPE TLTAATRSEE VRKKPEPPGS GRLAEGVKKK ILSRVAALRL
KLEEKENASF LKKMPKLETS LSCTEEKQDL TKPSCKREGR APVLLKKIQA EMSPECSGNV
KLSCQFAEIH EDSTICWTKD SKSIAQVQRS AGDNSTVSFA IVQASQKDQG LYYCCIKNSY
GKVTAEFNLT AEVLKQLSSH QDTKGCEEIE FSQLIFREDF LHDSYFGGRL RGQIATEELH
FGEGVHRKAF RSTVLRGLTP VFKPGHACVL KVHNAIAYGT RNNDELIQRN YKLAAQECYV
QNTARYYAKI YAAEAQPLEG FGEVPEIIPI FLIHRPENNI PYATVEEELI GEFVKYSIRD
GKEINFLRRE SEAGQKCCTF QHWVYQKTSG CLLVTDMQGV GMKLTDVGIA TLAKGYKGFK
GNCSMTFIDQ FKALHQCNKY CKMLGLKSLQ NNNQKQKKPS IGNCKVQANS GTGKKAGPET
PGEKKT
//
