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Database: UniProt
Entry: G1P5B1_MYOLU
LinkDB: G1P5B1_MYOLU
Original site: G1P5B1_MYOLU 
ID   G1P5B1_MYOLU            Unreviewed;      1670 AA.
AC   G1P5B1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Alpha kinase 3 {ECO:0000313|Ensembl:ENSMLUP00000005189.2};
GN   Name=ALPK3 {ECO:0000313|Ensembl:ENSMLUP00000005189.2};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000005189.2, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000005189.2, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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:ENSMLUP00000005189.2}
RP   IDENTIFICATION.
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}.
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DR   EMBL; AAPE02050466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02050467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02050468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 59463.ENSMLUP00000005189; -.
DR   Ensembl; ENSMLUT00000005680.2; ENSMLUP00000005189.2; ENSMLUG00000005659.2.
DR   eggNOG; ENOG502QPP5; Eukaryota.
DR   GeneTree; ENSGT00940000158534; -.
DR   InParanoid; G1P5B1; -.
DR   OMA; WPPAINR; -.
DR   TreeFam; TF332629; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
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:UP000001074};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          70..166
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1240..1328
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1356..1590
FT                   /note="Alpha-type protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS51158"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          297..802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          824..917
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          943..965
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1022..1236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1593..1670
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..220
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..331
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..357
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..390
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..437
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..513
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..585
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..640
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..676
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..725
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..863
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        880..895
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1126..1158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1216..1236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1611..1670
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1670 AA;  177960 MW;  D8C71D255D0B1871 CRC64;
     GKGEGGQVGE WEGDGKDKGR KLWXPSPTSR SYLLGVRPET SLSSSRLSLP SSGRSTFCSI
     IAQLTEETQP VFETTLKSQA VSKDSDVRFT CIITGYPEPE VTWYKDDTEL DRFCGLPKYE
     ITHQGKRHTL QLYRCQEEDA AIYQASARNT KGIVSCSGVL EVGTMTEYKI HQRWFAKLKC
     KAEAKMREIE QSWKRGKEVA GEADTLRKLS PDRFQRKRRL SGAEMPVPSA PTREAEDRTS
     ATWQERETEP GQHPGLSLIN SFAPGEVTTN GDAVPENGED GDHGLLTYIC EAMELGPQRA
     PQKELGAKKK KKVEEPKPGL RKPELEKAAR GDCSENCVPS SDKPDSCGTQ GPVDAEQIQT
     WSRGRAARGP GSSGVESTRK PASAMGSPAQ AQNVPAPAPG PDQEVYFSLK DMYLESTQAV
     RPQGEQGYHT QSGRESREMP SGKVPSEAKS EKGPPAPDQP IPSAPQPTRP FNRKRFAPPK
     PKGEPTTNSK PDSSLNQAPE PGAQSLGNGP PQASAQVPTP PARRRHSTRD SPLQGQAGRR
     TPGEVPESQA TMVPTVWASS SIGIASAGGS TPRSQSIIEP MDTETQESRT YADWRHGGMK
     NTEADGKMQV DGRTQADRKT QMDIVTQESE RTESDRSSQK DVVAQGRTGT QAERTQEDRK
     TQAGAKTQED RIQEGRGTQT EGSVPTTVKV QSEKKSVTNL SPQSRAPEPS PSEGSSSQII
     ACFEQSPERS SVPEKPGFML RSGEAAETAS RNQEETVLGP LSGGLRLPAQ LLPESGLEQT
     GGGRCWGPEW SGPVKDKPED SLFQCPKKEQ LGEVLSVDLG GCPPAGLSPD VPTLPSPAGA
     GLTDSSPQGL PSTPTSQHMS AAAFLPSGDQ ALRNSAPSVH LGPGTPTQNH PPETIAASNE
     GACAKMSDVE GRPSGTQSCD PGLIDSLKNY LLLLLKLSST ETSRGGTKSQ EAAAPRGLAP
     SPTLAPTLEV AGLSPQTSRR ILERVENDHL VQSAQMLLLS PCTSRRITGL LDREVQAGQQ
     ALAAARSPGS SPLTVPAIVV GEEEDPGLTS EGSSKGDGEV PLARSGLLGT SQESSAGGLL
     GEAGGQAASG QGPLSAESRV QDPSREEEIP QEAPAGLPAA TPEELALGAR RKRFLPKARA
     AGDGEATKPE ERESPTVSPR GPRKGLSPGS PGTLGREKRS PTQGRKAGLL EVPQAEEEQA
     AGDLGSSPKP SGLDAEPTLD EGKQETPGKP RKAKDLLKAP QVIRKIRVEQ FPDASGSLKL
     WCQFFNILSD SVLTWAKDLH PVGEVGRSAG DEGPAALAIV QASPGDCGMY RCTIHNEHGS
     ASTDFCLSPE VLSGFISREE GEVGEEIEMT PMVFAKGLAD SGCWGDKLFG RLVSEDLRGG
     GHRYSLRKAS QAKVIYGLEP IFESGRTCVI KVSSPLVFGP SSETSLLGRN YDVTIQGCKI
     QNMSREYCKI FAAEARAAPG FGEVPEIIPL YLIYRPANNI PYATLEEDLG KPLEPYCSRE
     WGCAAAPASG SSEAVQKCQA FQHWLYLWTN GSFLVTDLAG VDWKMTDVQI ATKLRGYQGL
     KESCFPALLD QFASSHKCNT FCEMLGLKPL KGPEAAHSQV KAKGSKSPSA GRKGPQLSPQ
     PQKKGLPSPQ GSRKSTPSSK ATPQASGAVA TQLLGQPPSQ EGGSKAQGTR
//
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