ID M7BTN2_CHEMY Unreviewed; 1303 AA.
AC M7BTN2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Phosphorylase b kinase regulatory subunit {ECO:0000256|RuleBase:RU364123};
GN ORFNames=UY3_03650 {ECO:0000313|EMBL:EMP39145.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP39145.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of
CC serine in certain substrates, including troponin I. The alpha chain may
CC bind calmodulin. {ECO:0000256|ARBA:ARBA00002837}.
CC -!- PATHWAY: Glycan biosynthesis; glycogen metabolism.
CC {ECO:0000256|ARBA:ARBA00005131, ECO:0000256|RuleBase:RU364123}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004342,
CC ECO:0000256|RuleBase:RU364123}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004342, ECO:0000256|RuleBase:RU364123};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342,
CC ECO:0000256|RuleBase:RU364123}. Membrane
CC {ECO:0000256|ARBA:ARBA00004423}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004423}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004423}.
CC -!- SIMILARITY: Belongs to the phosphorylase b kinase regulatory chain
CC family. {ECO:0000256|ARBA:ARBA00007128, ECO:0000256|RuleBase:RU364123}.
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DR EMBL; KB517472; EMP39145.1; -; Genomic_DNA.
DR STRING; 8469.M7BTN2; -.
DR eggNOG; KOG3635; Eukaryota.
DR UniPathway; UPA00163; -.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011613; GH15-like.
DR InterPro; IPR045583; KPBA/B_C.
DR InterPro; IPR008734; PHK_A/B_su.
DR PANTHER; PTHR10749; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR10749:SF4; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT ALPHA, SKELETAL MUSCLE ISOFORM; 1.
DR Pfam; PF00723; Glyco_hydro_15; 1.
DR Pfam; PF19292; KPBB_C; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 3: Inferred from homology;
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860,
KW ECO:0000256|RuleBase:RU364123};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU364123};
KW Cell membrane {ECO:0000256|RuleBase:RU364123};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600,
KW ECO:0000256|RuleBase:RU364123}; Kinase {ECO:0000313|EMBL:EMP39145.1};
KW Lipoprotein {ECO:0000256|RuleBase:RU364123};
KW Membrane {ECO:0000256|RuleBase:RU364123};
KW Prenylation {ECO:0000256|RuleBase:RU364123};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Transferase {ECO:0000313|EMBL:EMP39145.1}.
FT DOMAIN 37..977
FT /note="GH15-like"
FT /evidence="ECO:0000259|Pfam:PF00723"
FT DOMAIN 1088..1183
FT /note="Phosphorylase b kinase regulatory subunit alpha/beta
FT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19292"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1278
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1303 AA; 145699 MW; 4E3D27B221425179 CRC64;
MELKLKELED HEKERQDRER QRQHELAMVQ LRSRETPAGD PVTGLLPASS DHKDAWVRDN
VYSVLSMWGL GLAYRKNADR DEDKAKAYEL EQSVVKLMRG LLQCMMRQVD KVEAFKYSQS
PKDCFHAKYN THTCATVVGD DQWGHLQLDA TSIYLLMLAQ MTASGLHIIY SLDEVNFIQN
VVFYIEAAYK TADFGIWERG DKTNQGITEL NVSSIGMAKA ALEALDELDL FGAKGGPQSV
IHVLTDEVQH CQRGLIPDRA ALVSGLVYTV RGDQSKLRNF SYVNNIAEVN VLRSTHCGVC
LLWASTSKEI DASLLSVISY PAFAVEDSEL VEITKQEIVT KLQGRYGCCR FLRDGYRTPR
EDPNRLYYEP AELKLFENIE CEWPLFWTYF IIDGLFSGNV EQVQEYREAL EGVLIKGKNG
VRMVPELYSV PPNKVDEEYM NPHTVDRVPM GKLPHMWGQS LYILGCLMAE GFLAPGEIDP
LNRRFATVPK PDVVVQVCIL AETDGIKAIL KKQGIEVETV ADVYPIRVQP ARILSHIYAR
LGRNKQMNLS GRPFRYMGVL GTSKLYDIRK NIFTFTPQFI DQQQFYLALD NKMIVEMLRT
DLSYLCSCWR MTGRPTITFP ISQTMLVTDD TGTSIHPTVL AMLRKLKDGY FGGARTQTGK
LSEFLTTSCC THLSFMDPGP EGKLYADDYG LSIDSYSELD PEEWLHGFQL ASDADVCDEV
AQYLDHLLEH TAPKAAQKGG LHRFRAAVHT TCDLMSLVSQ AKELHVQNVN MYIPSKLFQA
SQPSVHLLGS THTPEQDSQI PSLHTMVNLP RDKAGNVDCK ALVDQLRECP TLQEQADLLY
MLHTLKGLDW DLEIDGQPGA TVKDLLTELY VNVGATRQWA LIRYISGILK KKVEALDEAC
TDLLSHQKHL TVGLPPEPRE KTISAPVPYE ELTRLIDEAS EKNMSVSILT QEIMVYLAMY
IRTQPALFAE MFRLRIGLII QVMATELAHS LHCSAEEATE SLMNLSPSDM KSLLHHILSG
KEFGVEKRVR SVDSALTPAI SIREVGAVGA TKTERAGIVK LKSEIKQSSG NSFLPAGGSF
ASMLEDQVSR DGRHGQWQRR RRLDGALNRV PVGFYQKVWK ILQKCHGLSV EGFVLPASTT
KEMTPGEIKF SVHVESVLNR VPQPEYRQLL VEAILVLTML ADVEIHSIGG IIAVEKIVHI
ANDLFCEEQK ALGADDNMLQ KDPATGICTL LYDSAPSGRF GTMTYLSRAV ATTSEPSNPP
CSLSPDRPPR PSAPYPTPRP QAGTLNAAQS SMSEPDALIR QSA
//
