ID V5GXR8_ANOGL Unreviewed; 268 AA.
AC V5GXR8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Phosphorylase b kinase regulatory subunit {ECO:0000256|RuleBase:RU364123};
DE Flags: Fragment;
GN Name=KPBB {ECO:0000313|EMBL:JAB66592.1};
OS Anoplophora glabripennis (Asian longhorn beetle) (Anoplophora nobilis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Chrysomeloidea; Cerambycidae; Lamiinae; Lamiini; Anoplophora.
OX NCBI_TaxID=217634 {ECO:0000313|EMBL:JAB66592.1};
RN [1] {ECO:0000313|EMBL:JAB66592.1}
RP NUCLEOTIDE SEQUENCE.
RA Scully E.D., Hoover K., Carlson J.E., Tien M., Geib S.M.;
RT "Midgut Transcriptome Profiling of Anoplphora glabripennis, a
RT Lignocellulose Degrading, Wood-Boring Cerambycid.";
RL Submitted (JUL-2013) 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|RuleBase:RU364123}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU364123};
CC Lipid-anchor {ECO:0000256|RuleBase:RU364123}; Cytoplasmic side
CC {ECO:0000256|RuleBase:RU364123}.
CC -!- SIMILARITY: Belongs to the phosphorylase b kinase regulatory chain
CC family. {ECO:0000256|RuleBase:RU364123}.
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DR EMBL; GALX01001874; JAB66592.1; -; Transcribed_RNA.
DR AlphaFoldDB; V5GXR8; -.
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: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 InterPro; IPR011613; GH15-like.
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.
PE 3: Inferred from homology;
KW Calmodulin-binding {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|RuleBase:RU364123};
KW Kinase {ECO:0000313|EMBL:JAB66592.1};
KW Lipoprotein {ECO:0000256|RuleBase:RU364123};
KW Membrane {ECO:0000256|RuleBase:RU364123};
KW Prenylation {ECO:0000256|RuleBase:RU364123};
KW Transferase {ECO:0000313|EMBL:JAB66592.1}.
FT DOMAIN 82..210
FT /note="GH15-like"
FT /evidence="ECO:0000259|Pfam:PF00723"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:JAB66592.1"
FT NON_TER 268
FT /evidence="ECO:0000313|EMBL:JAB66592.1"
SQ SEQUENCE 268 AA; 30870 MW; F3FACF9DC0080164 CRC64;
GTFGISMDAL DYPTDDFNQF MQLEHDYIGY QSLTDIPRVL NYQDELKDYS HFKNKSTNEI
IEAIKNIESI YARCQLFGIL LNREGSDFMM QDLTVEDHLQ GLYHKAGGLR HWAAVRYISS
LLHHTVDSIS PFITAVLVHG KQLTVGVIGQ KETVFDKPMT PAEIQAVVYN TIQPYDVIQA
VLQQEVILYC GRLIGTNPEL FHGILKFRVG WVLEAIKYYL QIFGDKKKIE DHSPYEVRQL
LFKVLSIKEW GAKEQLTPRQ KRQLEGCL
//
