ID Q4S8G1_TETNG Unreviewed; 1080 AA.
AC Q4S8G1;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Phosphorylase b kinase regulatory subunit {ECO:0000256|RuleBase:RU364123};
DE Flags: Fragment;
GN ORFNames=GSTENG00022351001 {ECO:0000313|EMBL:CAG03071.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|EMBL:CAG03071.1};
RN [1] {ECO:0000313|EMBL:CAG03071.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|EMBL:CAG03071.1}
RP NUCLEOTIDE SEQUENCE.
RG Genoscope;
RG Whitehead Institute Centre for Genome Research;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of
CC serine in certain substrates, including troponin I.
CC {ECO:0000256|RuleBase:RU364123}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CAG03071.1}.
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DR EMBL; CAAE01014706; CAG03071.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4S8G1; -.
DR KEGG; tng:GSTEN00022351G001; -.
DR BRENDA; 2.7.11.19; 9550.
DR UniPathway; UPA00163; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR008928; 6-hairpin_glycosidase_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:SF8; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT BETA; 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};
KW Lipoprotein {ECO:0000256|RuleBase:RU364123};
KW Membrane {ECO:0000256|RuleBase:RU364123};
KW Prenylation {ECO:0000256|RuleBase:RU364123}.
FT DOMAIN 2..867
FT /note="GH15-like"
FT /evidence="ECO:0000259|Pfam:PF00723"
FT DOMAIN 907..1048
FT /note="Phosphorylase b kinase regulatory subunit alpha/beta
FT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19292"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAG03071.1"
FT NON_TER 1080
FT /evidence="ECO:0000313|EMBL:CAG03071.1"
SQ SEQUENCE 1080 AA; 123289 MW; 1A2E899AF726F185 CRC64;
LVKTTILNYQ SPTTGLFPVK TCSTCKEAKV RDSLYCAASA WALAMAYRRI DDDMGRNHEL
EHSAVKCMRG ILYCYMRQAD TVEQFKQDPS PTKCLHSVFN VDTGDEVHAY KDYHHLQIDA
VSLFLLYLVE MICSGLQIIY NTDEIRSQPS WHYCQLFHPF EFFSWKIWQI GKRNKTKLFH
SNSVGLAKAA LEAINGFNLF GNQGCSWSVI FVDLDAHNRN RQTLSSLLPR ESRSHNTDAA
LLPTISYPAF AVDDDALYSQ TLDKIVRKLR GKYGFKRFLR DGYRTTNEDK NRRYYKPAEM
KTLLGVEVFH SYQALKAMAG VHVLGRSWSN NSATKLRPPA TARGQRASER WSVISQQLFD
GIECEFPIFF IYMMIDGHAI IPKYYYVPAD FVEAEQSKHG SQKRFPSNSG HDGNIFLWGQ
ALYNLAKLLV DELISPKDID PVHRYVPRQD QRNVSMRYSN QALLQSLWQE PLVSRGPIEN
DVMIHVALIA ESQRLQVFLN TYGIQTQTPQ QVEPIQIWPQ KELVKAYRFL AVNKKLGLSG
RPERPVGCIG TCKIYRILGK TVVCYPIVFD LSDFYLSQDV MLLIDDIKNA LQFIKQCWKM
QGRPLFLVLI REDNIKGSRF NPVLDMLASF KKGNVGGVKV HVDRLQTLIS GAVVEQLDFL
RVNEAEIPEF KSFEELELPK HSKVKRQMST PNASDLEQQP EISEEEWLHK PTQEIIQKFH
DCACLASQAQ LAGILLRREG PQFLSRDETM KDELERIYRR AGSRKLWLAV RQAAVVLEKF
ASSIAPHITT ILVHGKQVTL GLFGQQEEVI SNPLSPGVIQ GIIYSKCSAQ GAEREAVLQQ
ELVIHIGWII SNNPELFSGM LKIRVGWIVQ AMKHELKIRA GDMPPQDIHQ LSPSDIKQLL
LDVLQPQHTG RSWLNRRQID GSLNRTPLGF YDRVWQILER TSNGIVVAGT HLPQQPTLSD
MTMYEMNFSL LVEDTLKNIV LPEYRQVILL MVVSIVLERN PELEFSDKVD LDGLVKEAFN
DFQRDRSRFE GIEKQDVMEA FYNTPPTGKR GTSSYLTKAV MIQLLAGDVK PCKDDPCSVS
//
