ID A0A087QXF3_APTFO Unreviewed; 1202 AA.
AC A0A087QXF3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Phosphorylase b kinase regulatory subunit {ECO:0000256|RuleBase:RU364123};
DE Flags: Fragment;
GN ORFNames=AS27_07534 {ECO:0000313|EMBL:KFM05907.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM05907.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM05907.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM05907.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- PTM: Although the final Cys may be farnesylated, the terminal
CC tripeptide is probably not removed, and the C-terminus is not
CC methylated. {ECO:0000256|PIRSR:PIRSR608734-50}.
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; KL225966; KFM05907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087QXF3; -.
DR STRING; 9233.A0A087QXF3; -.
DR UniPathway; UPA00163; -.
DR Proteomes; UP000053286; 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:SF5; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT ALPHA, LIVER 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:KFM05907.1};
KW Lipoprotein {ECO:0000256|PIRSR:PIRSR608734-50,
KW ECO:0000256|RuleBase:RU364123}; Membrane {ECO:0000256|RuleBase:RU364123};
KW Prenylation {ECO:0000256|PIRSR:PIRSR608734-50,
KW ECO:0000256|RuleBase:RU364123};
KW Reference proteome {ECO:0000313|Proteomes:UP000053286};
KW Transferase {ECO:0000313|EMBL:KFM05907.1}.
FT DOMAIN 1..889
FT /note="GH15-like"
FT /evidence="ECO:0000259|Pfam:PF00723"
FT DOMAIN 1028..1118
FT /note="Phosphorylase b kinase regulatory subunit alpha/beta
FT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19292"
FT REGION 946..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1025
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1199
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000256|PIRSR:PIRSR608734-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM05907.1"
FT NON_TER 1202
FT /evidence="ECO:0000313|EMBL:KFM05907.1"
SQ SEQUENCE 1202 AA; 134846 MW; BC4DBB4B6FC8D87C CRC64;
NPVTGLLSAG TDHKDAWVRD NIYSILAVWG LGMAYRKNAD RDEDKAKAYE LEQNVVKLMR
GLLQCMMRQV DKVEKFKRTQ STKDCLHAKY NSATCATVVG DDQWGHLQVD ATSLYLLFLA
QMTASGLRII FTLDEVTFIQ NLVFYIEAAY KVADYGIWER GDKTNQGIPE LNASSVGMAK
AALEAIDELD LFGAHGGHKS VIHVLPDEVE HCQSILYSML PRASTSKEID AGLLSIISYP
AFAVEDLNLV NVTKSEIISK LQGRYGCCRF LRDGYKTPRE DPSRLHYDPA ELKLFENIEC
EWPVFWTYFL IDGVFNEDKI QVQEYREALE GILIREKNGI VLMPELYAVP PEKVDEEYEN
PHSVDRIPVG KLPHLWGQSL YVLSCLLAEG FLAVGEIDPL NRRFSTGFKP DVVVQVTVLA
ESNQIKNLLQ DRGINVQSIA DIHPLRVQPA RILSNLYTML GRNKNMKLSG RPHRHIGVLG
TSKLYMIRNQ IFAFTPQFTD QHHFYLALDN QMIVEMLKTE LAYLTSCWRM TGRPTLTFPI
THTMLVDDGT DIHPAVLATI RKLEDGYFGG ARVKIGKLSE FLTTSFHTYL SFLDPDCDIK
LFDGPNEGRN SPDSEYGGYP ADFCEKESQD ELDQYINDVL QSTALKSYLP PTSKTVNQSP
VFSANHSTKE ILSIMAKTKG LEVPAVSMSL PTKVLNNRKS LNLVDNPHFF ETKDCENVLH
LPKDAHGDLD CRKLVEQLKE CPTLHDQADI LYILHMLKGA DWDTELDGQY GVTVHCLLNE
LYRKAGLNQE WGLIRYISGI LKKRVEVLAE ACTDLLSHHK QLTVGLPPEP REKIITTPLP
PEQLTDLIYE ASGQDISIAV LTQEIIMYLA MYVRSQPSLF VEMLRLRIGL IIQVMATELA
RSLKCSGEEA SESLMNLSPF DMKNLLHHIL SGKEFGVERS LRPVDSSSSS PAISIHEMGH
SGATKTERSG ITKLKSEMKQ VRGFCQRLSE NAAVLVLCYV GFLCRGSTPS SPTSTSPTGS
KGETSWGDRK GQWLRRRRLD GAINRVPVGF YEKVWKILQK CHGLSIDGYV LPSSTTREMT
PCEIKFAVHV ESVLNHVPQP EYRQLLVEAI LVLTFLSDIE VNSIGGIIHV DRIVHVANDL
FLQELKSFGA TGSILEKDVA TGICHFFYDS APSGAYGTMT YLTKAIIIYL HDFLPSTGCA
MQ
//
