GLYG_RABIT
ID GLYG_RABIT Reviewed; 333 AA.
AC P13280;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Glycogenin-1;
DE Short=GN-1;
DE Short=GN1;
DE EC=2.4.1.186 {ECO:0000269|PubMed:1281472, ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22128147, ECO:0000269|PubMed:22226635, ECO:0000269|PubMed:2526735};
GN Name=GYG1; Synonyms=GYG;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, PATHWAY, AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=1281472; DOI=10.1016/s0021-9258(18)35674-6;
RA Viskupic E., Cao Y., Zhang W., Cheng C., Depaoli-Roach A.A., Roach P.J.;
RT "Rabbit skeletal muscle glycogenin. Molecular cloning and production of
RT fully functional protein in Escherichia coli.";
RL J. Biol. Chem. 267:25759-25763(1992).
RN [2]
RP PROTEIN SEQUENCE OF 2-333.
RC STRAIN=New Zealand white; TISSUE=Skeletal muscle;
RX PubMed=2806254; DOI=10.1111/j.1432-1033.1989.tb15090.x;
RA Campbell D.G., Cohen P.;
RT "The amino acid sequence of rabbit skeletal muscle glycogenin.";
RL Eur. J. Biochem. 185:119-125(1989).
RN [3]
RP PROTEIN SEQUENCE OF 35-48; 182-202; 210-227 AND 308-325, FUNCTION,
RP CATALYTIC ACTIVITY, PATHWAY, AND COFACTOR.
RC TISSUE=Liver;
RX PubMed=2526735; DOI=10.1111/j.1432-1033.1989.tb14914.x;
RA Smythe C., Villar-Palasi C., Cohen P.;
RT "Structural and functional studies on rabbit liver glycogenin.";
RL Eur. J. Biochem. 183:205-209(1989).
RN [4]
RP PROTEIN SEQUENCE OF 35-48, AND PHOSPHORYLATION AT SER-44.
RX PubMed=3151442;
RA Lomako J., Whelan W.J.;
RT "The occurrence of serine phosphate in glycogenin: a possible regulatory
RT site.";
RL BioFactors 1:261-264(1988).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, GLYCOSYLATION AT TYR-195, AND
RP MUTAGENESIS OF TYR-195.
RX PubMed=8143846; DOI=10.1016/0014-5793(94)80580-6;
RA Alonso M.D., Lomako J., Lomako W.M., Whelan W.J.;
RT "Tyrosine-194 of glycogenin undergoes autocatalytic glucosylation but is
RT not essential for catalytic function and activity.";
RL FEBS Lett. 342:38-42(1994).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT TYR-195, AND MUTAGENESIS OF
RP TYR-195.
RX PubMed=7771798; DOI=10.1006/abbi.1995.1295;
RA Cao Y., Steinrauf L.K., Roach P.J.;
RT "Mechanism of glycogenin self-glucosylation.";
RL Arch. Biochem. Biophys. 319:293-298(1995).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT TYR-195, AND MUTAGENESIS OF
RP LYS-86 AND TYR-195.
RX PubMed=10049511; DOI=10.1006/abbi.1998.1073;
RA Lin A., Mu J., Yang J., Roach P.J.;
RT "Self-glucosylation of glycogenin, the initiator of glycogen biosynthesis,
RT involves an inter-subunit reaction.";
RL Arch. Biochem. Biophys. 363:163-170(1999).
RN [8] {ECO:0007744|PDB:1LL0, ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1LL3}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH UDP-GLUCOSE AND
RP MANGANESE IONS, SUBUNIT, AND COFACTOR.
RX PubMed=12051921; DOI=10.1016/s0022-2836(02)00305-4;
RA Gibbons B.J., Roach P.J., Hurley T.D.;
RT "Crystal structure of the autocatalytic initiator of glycogen biosynthesis,
RT glycogenin.";
RL J. Mol. Biol. 319:463-477(2002).
RN [9] {ECO:0007744|PDB:1ZCT, ECO:0007744|PDB:1ZCU, ECO:0007744|PDB:1ZCV, ECO:0007744|PDB:1ZCY, ECO:0007744|PDB:1ZDF, ECO:0007744|PDB:1ZDG}
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH MANGANESE; UDP AND
RP UDP-ALPHA-D-GLUCOSE, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, COFACTOR,
RP SUBUNIT, AND MUTAGENESIS OF ASP-160 AND ASP-163.
RX PubMed=15849187; DOI=10.1074/jbc.m502344200;
RA Hurley T.D., Stout S., Miner E., Zhou J., Roach P.J.;
RT "Requirements for catalysis in mammalian glycogenin.";
RL J. Biol. Chem. 280:23892-23899(2005).
RN [10] {ECO:0007744|PDB:3V8Y, ECO:0007744|PDB:3V8Z, ECO:0007744|PDB:3V90, ECO:0007744|PDB:3V91}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-271 OF WILD-TYPE AND MUTANT
RP MET-83 IN COMPLEX WITH MANGANESE; UDP AND UDP-ALPHA-D-GLUCOSE, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND MUTAGENESIS OF THR-83.
RX PubMed=22226635; DOI=10.1016/j.febslet.2011.12.028;
RA Carrizo M.E., Romero J.M., Issoglio F.M., Curtino J.A.;
RT "Structural and biochemical insight into glycogenin inactivation by the
RT glycogenosis-causing T82M mutation.";
RL FEBS Lett. 586:254-257(2012).
RN [11] {ECO:0007744|PDB:3USQ, ECO:0007744|PDB:3USR}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-271, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF TYR-195, AND GLYCOSYLATION AT
RP TYR-195.
RX PubMed=22128147; DOI=10.1074/jbc.m111.287813;
RA Issoglio F.M., Carrizo M.E., Romero J.M., Curtino J.A.;
RT "Mechanisms of monomeric and dimeric glycogenin autoglucosylation.";
RL J. Biol. Chem. 287:1955-1961(2012).
CC -!- FUNCTION: Self-glucosylates, via an inter-subunit mechanism, to form an
CC oligosaccharide primer that serves as substrate for glycogen synthase.
CC {ECO:0000269|PubMed:10049511, ECO:0000269|PubMed:1281472,
CC ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22128147,
CC ECO:0000269|PubMed:22226635, ECO:0000269|PubMed:2526735,
CC ECO:0000269|PubMed:7771798, ECO:0000269|PubMed:8143846}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = alpha-D-
CC glucosyl-L-tyrosyl-[glycogenin] + H(+) + UDP; Xref=Rhea:RHEA:23360,
CC Rhea:RHEA-COMP:14604, Rhea:RHEA-COMP:14605, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:140573; EC=2.4.1.186;
CC Evidence={ECO:0000269|PubMed:10049511, ECO:0000269|PubMed:1281472,
CC ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22128147,
CC ECO:0000269|PubMed:22226635, ECO:0000269|PubMed:2526735,
CC ECO:0000269|PubMed:7771798, ECO:0000269|PubMed:8143846};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[1,4-alpha-D-glucosyl](n)-L-tyrosyl-[glycogenin] + UDP-alpha-
CC D-glucose = [1,4-alpha-D-glucosyl](n+1)-L-tyrosyl-[glycogenin] + H(+)
CC + UDP; Xref=Rhea:RHEA:56560, Rhea:RHEA-COMP:14606, Rhea:RHEA-
CC COMP:14607, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:140574; EC=2.4.1.186;
CC Evidence={ECO:0000269|PubMed:10049511, ECO:0000269|PubMed:1281472,
CC ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22128147,
CC ECO:0000269|PubMed:22226635, ECO:0000269|PubMed:2526735,
CC ECO:0000269|PubMed:7771798, ECO:0000269|PubMed:8143846};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12051921, ECO:0000269|PubMed:1281472,
CC ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22128147,
CC ECO:0000269|PubMed:22226635, ECO:0000269|PubMed:2526735,
CC ECO:0000269|PubMed:8143846};
CC Note=Divalent metal ions. Required for self-glucosylation. Manganese is
CC the most effective. {ECO:0000269|PubMed:12051921};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000269|PubMed:1281472, ECO:0000269|PubMed:15849187,
CC ECO:0000269|PubMed:2526735}.
CC -!- SUBUNIT: Homodimer (PubMed:12051921, PubMed:15849187, PubMed:22226635,
CC PubMed:22128147). Interacts (via C-terminus) with glycogen synthase
CC GYS1 (By similarity). Interacts (via C-terminus) with glycogen synthase
CC GYS2 (By similarity). This interaction is required for GYS2-mediated
CC glycogen synthesis (By similarity). {ECO:0000250|UniProtKB:P46976,
CC ECO:0000250|UniProtKB:Q9R062, ECO:0000269|PubMed:12051921,
CC ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22128147,
CC ECO:0000269|PubMed:22226635}.
CC -!- TISSUE SPECIFICITY: Detected in heart, skeletal muscle, brain and
CC testis, and at lower levels in kidney. {ECO:0000269|PubMed:1281472}.
CC -!- PTM: Self-glycosylated by the transfer of glucose residues from UDP-
CC glucose to itself, forming an alpha-1,4-glycan of around 10 residues
CC attached to Tyr-195. {ECO:0000269|PubMed:10049511,
CC ECO:0000269|PubMed:22128147, ECO:0000269|PubMed:22226635,
CC ECO:0000269|PubMed:7771798, ECO:0000269|PubMed:8143846}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:3151442}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. Glycogenin
CC subfamily. {ECO:0000305}.
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DR EMBL; L01791; AAA31404.1; -; mRNA.
DR PIR; A45094; A45094.
DR RefSeq; NP_001075710.1; NM_001082241.1.
DR PDB; 1LL0; X-ray; 3.43 A; A/B/C/D/E/F/G/H/I/J=1-333.
DR PDB; 1LL2; X-ray; 1.90 A; A=1-333.
DR PDB; 1LL3; X-ray; 1.90 A; A=1-333.
DR PDB; 1ZCT; X-ray; 2.60 A; A/B=1-270.
DR PDB; 1ZCU; X-ray; 2.00 A; A=1-333.
DR PDB; 1ZCV; X-ray; 1.98 A; A=1-333.
DR PDB; 1ZCY; X-ray; 1.99 A; A=1-333.
DR PDB; 1ZDF; X-ray; 2.45 A; A=1-333.
DR PDB; 1ZDG; X-ray; 2.30 A; A=1-333.
DR PDB; 3USQ; X-ray; 2.40 A; A=1-271.
DR PDB; 3USR; X-ray; 2.10 A; A=1-271.
DR PDB; 3V8Y; X-ray; 2.15 A; A=1-271.
DR PDB; 3V8Z; X-ray; 2.20 A; A=1-271.
DR PDB; 3V90; X-ray; 2.00 A; A=1-271.
DR PDB; 3V91; X-ray; 2.00 A; A=1-271.
DR PDBsum; 1LL0; -.
DR PDBsum; 1LL2; -.
DR PDBsum; 1LL3; -.
DR PDBsum; 1ZCT; -.
DR PDBsum; 1ZCU; -.
DR PDBsum; 1ZCV; -.
DR PDBsum; 1ZCY; -.
DR PDBsum; 1ZDF; -.
DR PDBsum; 1ZDG; -.
DR PDBsum; 3USQ; -.
DR PDBsum; 3USR; -.
DR PDBsum; 3V8Y; -.
DR PDBsum; 3V8Z; -.
DR PDBsum; 3V90; -.
DR PDBsum; 3V91; -.
DR AlphaFoldDB; P13280; -.
DR SMR; P13280; -.
DR CORUM; P13280; -.
DR STRING; 9986.ENSOCUP00000019444; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR iPTMnet; P13280; -.
DR GeneID; 100009058; -.
DR KEGG; ocu:100009058; -.
DR CTD; 2992; -.
DR eggNOG; KOG1950; Eukaryota.
DR InParanoid; P13280; -.
DR OrthoDB; 1424146at2759; -.
DR BRENDA; 2.4.1.186; 1749.
DR UniPathway; UPA00164; -.
DR EvolutionaryTrace; P13280; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0008466; F:glycogenin glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0102751; F:UDP-alpha-D-glucose:glucosyl-glycogenin alpha-D-glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0005978; P:glycogen biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR002495; Glyco_trans_8.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF01501; Glyco_transf_8; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing;
KW Glycogen biosynthesis; Glycoprotein; Manganese; Metal-binding;
KW Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2806254"
FT CHAIN 2..333
FT /note="Glycogenin-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000215178"
FT REGION 284..316
FT /note="Interaction with GYS1"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 9..15
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12051921,
FT ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635,
FT ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZDF,
FT ECO:0007744|PDB:1ZDG, ECO:0007744|PDB:3V91"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 102..104
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12051921,
FT ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635,
FT ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZDF,
FT ECO:0007744|PDB:1ZDG, ECO:0007744|PDB:3V91"
FT BINDING 102
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:12051921,
FT ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635,
FT ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZCT,
FT ECO:0007744|PDB:1ZDF, ECO:0007744|PDB:1ZDG,
FT ECO:0007744|PDB:3V8Z, ECO:0007744|PDB:3V91"
FT BINDING 104
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:12051921,
FT ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635,
FT ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZCT,
FT ECO:0007744|PDB:1ZDF, ECO:0007744|PDB:1ZDG,
FT ECO:0007744|PDB:3V8Z, ECO:0007744|PDB:3V91"
FT BINDING 133..135
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12051921,
FT ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635,
FT ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZDF,
FT ECO:0007744|PDB:1ZDG, ECO:0007744|PDB:3V91"
FT BINDING 160..164
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12051921,
FT ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635,
FT ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZDF,
FT ECO:0007744|PDB:1ZDG, ECO:0007744|PDB:3V91"
FT BINDING 212..218
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12051921,
FT ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635,
FT ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZDF,
FT ECO:0007744|PDB:1ZDG, ECO:0007744|PDB:3V91"
FT BINDING 212
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:12051921,
FT ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635,
FT ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZCT,
FT ECO:0007744|PDB:1ZDF, ECO:0007744|PDB:1ZDG,
FT ECO:0007744|PDB:3V8Z, ECO:0007744|PDB:3V91"
FT SITE 86
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000269|PubMed:10049511"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT MOD_RES 44
FT /note="Phosphoserine; by PKA; in vitro"
FT /evidence="ECO:0000269|PubMed:3151442"
FT CARBOHYD 195
FT /note="O-linked (Glc...) tyrosine"
FT /evidence="ECO:0000269|PubMed:8143846"
FT MUTAGEN 83
FT /note="T->M: Loss of autoglucosylation."
FT /evidence="ECO:0000269|PubMed:22226635"
FT MUTAGEN 83
FT /note="T->S: No effect on autoglucosylation."
FT /evidence="ECO:0000269|PubMed:22226635"
FT MUTAGEN 86
FT /note="K->Q: Nearly abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:10049511"
FT MUTAGEN 160
FT /note="D->N,S: Reduced trans-glucosylation activity by at
FT least 260-fold and reduced UDP-glucose hydrolytic activity
FT by 4 to 14-fold."
FT /evidence="ECO:0000269|PubMed:15849187"
FT MUTAGEN 163
FT /note="D->N: Loss of self-glucosylation activity and
FT ability to trans-glucosylate maltose. Reduces UDP-glucose
FT hydrolytic activity by at least 190-fold."
FT /evidence="ECO:0000269|PubMed:15849187"
FT MUTAGEN 163
FT /note="D->S: Loss of self-glucosylation activity and 18 to
FT 30-fold reduction in its ability to trans-glucosylate
FT maltose. Reduces UDP-glucose hydrolytic activity by at
FT least 190-fold."
FT /evidence="ECO:0000269|PubMed:15849187"
FT MUTAGEN 195
FT /note="Y->F,T: Loss of self-glucosylation. No loss of
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:10049511,
FT ECO:0000269|PubMed:22128147, ECO:0000269|PubMed:7771798,
FT ECO:0000269|PubMed:8143846"
FT CONFLICT 39
FT /note="T -> L (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="C -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="C -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:1LL2"
FT HELIX 13..28
FT /evidence="ECO:0007829|PDB:1LL2"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:1LL2"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:1LL2"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:1LL2"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:1LL2"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1LL2"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:1LL2"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:1LL2"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:1LL2"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1LL2"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:1LL2"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:1LL2"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1LL2"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:1LL2"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:1LL2"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1ZCY"
FT HELIX 163..170
FT /evidence="ECO:0007829|PDB:1LL2"
FT TURN 171..176
FT /evidence="ECO:0007829|PDB:1LL2"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:1LL2"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:1LL2"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1LL2"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:1LL2"
FT HELIX 198..204
FT /evidence="ECO:0007829|PDB:1LL2"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:1LL2"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:1LL2"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1LL3"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:1LL2"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:3USR"
FT TURN 226..229
FT /evidence="ECO:0007829|PDB:1LL2"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:3USR"
FT HELIX 243..255
FT /evidence="ECO:0007829|PDB:1LL2"
FT HELIX 257..261
FT /evidence="ECO:0007829|PDB:1LL2"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:1ZCV"
SQ SEQUENCE 333 AA; 37397 MW; 7C27F7B428F67571 CRC64;
MTDQAFVTLT TNDAYAKGAL VLGSSLKQHR TSRRLAVLTT PQVSDTMRKA LEIVFDEVIT
VDILDSGDSA HLTLMKRPEL GVTLTKLHCW SLTQYSKCVF MDADTLVLAN IDDLFEREEL
SAAPDPGWPD CFNSGVFVYQ PSVETYNQLL HVASEQGSFD GGDQGLLNTF FNSWATTDIR
KHLPFIYNLS SISIYSYLPA FKAFGANAKV VHFLGQTKPW NYTYDTKTKS VRSEGHDPTM
THPQFLNVWW DIFTTSVVPL LQQFGLVQDT CSYQHVEDVS GAVSHLSLGE TPATTQPFVS
SEERKERWEQ GQADYMGADS FDNIKKKLDT YLQ
