PCY1A_RAT
ID PCY1A_RAT Reviewed; 367 AA.
AC P19836;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Choline-phosphate cytidylyltransferase A;
DE EC=2.7.7.15 {ECO:0000269|PubMed:12718547, ECO:0000269|PubMed:19783652, ECO:0000269|PubMed:2166941, ECO:0000269|PubMed:639816, ECO:0000269|PubMed:8185307, ECO:0000269|PubMed:8381041};
DE AltName: Full=CCT-alpha;
DE AltName: Full=CTP:phosphocholine cytidylyltransferase A;
DE Short=CCT A;
DE Short=CT A;
DE AltName: Full=Phosphorylcholine transferase A;
GN Name=Pcyt1a; Synonyms=Ctpct, Pcyt1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2166941; DOI=10.1073/pnas.87.16.6029;
RA Kalmar G.B., Kay R.J., Lachance A., Aebersold R., Cornell R.B.;
RT "Cloning and expression of rat liver CTP:phosphocholine
RT cytidylyltransferase: an amphipathic protein that controls
RT phosphatidylcholine synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6029-6033(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Lung;
RA Hogan M., Zimmermann L.J., Wang J., Kuliszewski M., Liu J., Buch S.,
RA Post M.;
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY
RP REGULATION.
RX PubMed=8381041; DOI=10.1006/prep.1993.1001;
RA Macdonald J.I.S., Kent C.;
RT "Baculovirus-mediated expression of rat liver CTP:phosphocholine
RT cytidylyltransferase.";
RL Protein Expr. Purif. 4:1-7(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=639816; DOI=10.1111/j.1432-1033.1978.tb12227.x;
RA Choy P.C., Schneider W.J., Vance D.E.;
RT "Immunological studies on CTP:phosphocholine cytidylyltransferase from the
RT livers of normal and choline-deficient rats.";
RL Eur. J. Biochem. 85:189-193(1978).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION, SUBCELLULAR LOCATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP SER-362.
RX PubMed=8185307; DOI=10.1006/abbi.1994.1215;
RA Sweitzer T.D., Kent C.;
RT "Expression of wild-type and mutant rat liver CTP: phosphocholine
RT cytidylyltransferase in a cytidylyltransferase-deficient Chinese hamster
RT ovary cell line.";
RL Arch. Biochem. Biophys. 311:107-116(1994).
RN [7]
RP PHOSPHORYLATION AT SER-315; SER-319; SER-321; SER-322; SER-323; SER-329;
RP SER-331; SER-333; SER-343; SER-345; SER-346; SER-347; SER-350; SER-352 AND
RP SER-362.
RC TISSUE=Liver;
RX PubMed=8144639; DOI=10.1016/s0021-9258(17)34092-9;
RA McDonald J.I.S., Kent C.;
RT "Identification of phosphorylation sites in rat liver CTP: phosphocholine
RT cytidylyltransferase.";
RL J. Biol. Chem. 269:10529-10537(1994).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-122.
RX PubMed=12718547; DOI=10.1021/bi027431+;
RA Helmink B.A., Braker J.D., Kent C., Friesen J.A.;
RT "Identification of lysine 122 and arginine 196 as important functional
RT residues of rat CTP:phosphocholine cytidylyltransferase alpha.";
RL Biochemistry 42:5043-5051(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319; SER-331; THR-342;
RP SER-347 AND SER-362, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [10]
RP STRUCTURE BY NMR OF 236-268.
RC TISSUE=Liver;
RX PubMed=8810902; DOI=10.1021/bi960821+;
RA Dunne S.J., Cornell R.B., Johnson J.E., Glover N.R., Tracey A.S.;
RT "Structure of the membrane binding domain of CTP:phosphocholine
RT cytidylyltransferase.";
RL Biochemistry 35:11975-11984(1996).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-236 IN COMPLEX WITH
RP CDP-CHOLINE, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-168 AND
RP TYR-173, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19783652; DOI=10.1074/jbc.m109.053363;
RA Lee J., Johnson J., Ding Z., Paetzel M., Cornell R.B.;
RT "Crystal structure of a mammalian CTP: phosphocholine cytidylyltransferase
RT catalytic domain reveals novel active site residues within a highly
RT conserved nucleotidyltransferase fold.";
RL J. Biol. Chem. 284:33535-33548(2009).
CC -!- FUNCTION: Catalyzes the key rate-limiting step in the CDP-choline
CC pathway for phosphatidylcholine biosynthesis.
CC {ECO:0000269|PubMed:12718547, ECO:0000269|PubMed:19783652,
CC ECO:0000269|PubMed:2166941, ECO:0000269|PubMed:639816,
CC ECO:0000269|PubMed:8185307, ECO:0000269|PubMed:8381041}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + H(+) + phosphocholine = CDP-choline + diphosphate;
CC Xref=Rhea:RHEA:18997, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:58779, ChEBI:CHEBI:295975;
CC EC=2.7.7.15; Evidence={ECO:0000269|PubMed:12718547,
CC ECO:0000269|PubMed:19783652, ECO:0000269|PubMed:2166941,
CC ECO:0000269|PubMed:639816, ECO:0000269|PubMed:8185307,
CC ECO:0000269|PubMed:8381041};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18998;
CC Evidence={ECO:0000305|PubMed:19783652};
CC -!- ACTIVITY REGULATION: By phosphorylation. Activated by N-
CC methylethanolamine (PubMed:8185307). Activated by oleic acid-containing
CC phosphatidylcholine vesicles (PubMed:8381041).
CC {ECO:0000269|PubMed:8185307, ECO:0000269|PubMed:8381041}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.41 uM for CTP {ECO:0000269|PubMed:8185307};
CC KM=0.47 uM for phosphocholine {ECO:0000269|PubMed:8185307};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphatidylcholine from phosphocholine: step 1/2.
CC {ECO:0000269|PubMed:12718547, ECO:0000269|PubMed:19783652,
CC ECO:0000269|PubMed:2166941, ECO:0000269|PubMed:639816,
CC ECO:0000269|PubMed:8185307, ECO:0000269|PubMed:8381041}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19783652}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:639816}.
CC Membrane {ECO:0000269|PubMed:639816}; Peripheral membrane protein
CC {ECO:0000269|PubMed:639816}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P49585}. Nucleus {ECO:0000269|PubMed:8185307}.
CC Note=It can interconvert between an inactive cytosolic form and an
CC active membrane-bound form.
CC -!- PTM: The serine residues of the C-terminus are phosphorylated. The
CC inactive soluble form is stabilized by phosphorylation, the active
CC membrane bound form is promoted by anionic lipids or diacylglycerol,
CC and is stabilized by dephosphorylation. {ECO:0000269|PubMed:8144639}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:2166941}.
CC -!- PTM: Monoubiquitinated by the SCF(FBXL2) complex, leading to
CC proteasomal degradation. {ECO:0000250|UniProtKB:P49586}.
CC -!- MISCELLANEOUS: The cytidylyltransferase may interact with membranes
CC through its amphipathic helix.
CC -!- SIMILARITY: Belongs to the cytidylyltransferase family. {ECO:0000305}.
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DR EMBL; M36071; AAA40995.1; -; mRNA.
DR EMBL; U03490; AAB60489.1; -; mRNA.
DR EMBL; L13245; AAB59683.1; -; mRNA.
DR EMBL; BC085713; AAH85713.1; -; mRNA.
DR PIR; A36001; A36001.
DR RefSeq; NP_511177.2; NM_078622.2.
DR RefSeq; XP_006248506.1; XM_006248444.3.
DR RefSeq; XP_008766916.1; XM_008768694.2.
DR PDB; 1PEH; NMR; -; A=236-268.
DR PDB; 1PEI; NMR; -; A=267-288.
DR PDB; 3HL4; X-ray; 2.20 A; A/B=1-236.
DR PDB; 4MVC; X-ray; 3.00 A; A/B=1-312.
DR PDB; 4MVD; X-ray; 8.00 A; A/B/C/D/E/F/G/H=1-312.
DR PDBsum; 1PEH; -.
DR PDBsum; 1PEI; -.
DR PDBsum; 3HL4; -.
DR PDBsum; 4MVC; -.
DR PDBsum; 4MVD; -.
DR AlphaFoldDB; P19836; -.
DR SMR; P19836; -.
DR STRING; 10116.ENSRNOP00000002403; -.
DR SwissLipids; SLP:000001188; -.
DR iPTMnet; P19836; -.
DR PhosphoSitePlus; P19836; -.
DR jPOST; P19836; -.
DR PaxDb; P19836; -.
DR PRIDE; P19836; -.
DR Ensembl; ENSRNOT00000002403; ENSRNOP00000002403; ENSRNOG00000001762.
DR GeneID; 140544; -.
DR KEGG; rno:140544; -.
DR UCSC; RGD:70515; rat.
DR CTD; 5130; -.
DR RGD; 70515; Pcyt1a.
DR eggNOG; KOG2804; Eukaryota.
DR GeneTree; ENSGT00940000157384; -.
DR HOGENOM; CLU_034585_4_2_1; -.
DR InParanoid; P19836; -.
DR OMA; RWPFSAK; -.
DR OrthoDB; 1172502at2759; -.
DR PhylomeDB; P19836; -.
DR TreeFam; TF106336; -.
DR BRENDA; 2.7.7.15; 5301.
DR Reactome; R-RNO-1483191; Synthesis of PC.
DR UniPathway; UPA00753; UER00739.
DR EvolutionaryTrace; P19836; -.
DR PRO; PR:P19836; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001762; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; P19836; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0019898; C:extrinsic component of membrane; NAS:RGD.
DR GO; GO:0042587; C:glycogen granule; ISO:RGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0005516; F:calmodulin binding; IDA:RGD.
DR GO; GO:0004105; F:choline-phosphate cytidylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008289; F:lipid binding; IMP:RGD.
DR GO; GO:0031210; F:phosphatidylcholine binding; IDA:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0006657; P:CDP-choline pathway; IDA:UniProtKB.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:UniProtKB.
DR CDD; cd02174; CCT; 1.
DR DisProt; DP02118; -.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR041723; CCT.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR045049; Pcy1-like.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR10739; PTHR10739; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Nucleotidyltransferase; Nucleus; Phospholipid biosynthesis;
KW Phospholipid metabolism; Phosphoprotein; Reference proteome; Repeat;
KW Transferase; Ubl conjugation.
FT CHAIN 1..367
FT /note="Choline-phosphate cytidylyltransferase A"
FT /id="PRO_0000208455"
FT REPEAT 319..324
FT /note="1"
FT REPEAT 329..333
FT /note="2; approximate"
FT REPEAT 343..348
FT /note="3"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..287
FT /note="Amphipathic"
FT /evidence="ECO:0000255"
FT REGION 256..288
FT /note="3 X 11 AA approximate tandem repeats"
FT REGION 298..315
FT /note="Amphipathic"
FT /evidence="ECO:0000255"
FT REGION 313..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..348
FT /note="3 X repeats"
FT COMPBIAS 7..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 84..92
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000269|PubMed:19783652,
FT ECO:0007744|PDB:3HL4, ECO:0007744|PDB:4MVC,
FT ECO:0007744|PDB:4MVD"
FT BINDING 122
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000269|PubMed:19783652,
FT ECO:0007744|PDB:3HL4, ECO:0007744|PDB:4MVC"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19783652,
FT ECO:0007744|PDB:3HL4, ECO:0007744|PDB:4MVC"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19783652,
FT ECO:0007744|PDB:3HL4"
FT BINDING 168..169
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000269|PubMed:19783652,
FT ECO:0007744|PDB:3HL4, ECO:0007744|PDB:4MVC"
FT BINDING 173
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000269|PubMed:19783652,
FT ECO:0007744|PDB:3HL4, ECO:0007744|PDB:4MVC"
FT BINDING 196..200
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000269|PubMed:19783652,
FT ECO:0007744|PDB:3HL4, ECO:0007744|PDB:4MVC,
FT ECO:0007744|PDB:4MVD"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P49585"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49585"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49585"
FT MOD_RES 315
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:8144639"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8144639,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8144639"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8144639"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8144639"
FT MOD_RES 325
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49586"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8144639"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8144639,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 333
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:8144639"
FT MOD_RES 342
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8144639"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8144639"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8144639"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8144639,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8144639"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8144639"
FT MOD_RES 358
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49586"
FT MOD_RES 362
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:8144639,
FT ECO:0007744|PubMed:22673903"
FT MUTAGEN 122
FT /note="K->A: Nearly abolishes enzyme activity. Decreases
FT affinity for phosphocholine about 500-fold."
FT /evidence="ECO:0000269|PubMed:12718547"
FT MUTAGEN 122
FT /note="K->R: Nearly abolishes enzyme activity. Decreases
FT affinity for phosphocholine about 80-fold."
FT /evidence="ECO:0000269|PubMed:12718547"
FT MUTAGEN 168
FT /note="H->A: Strongly reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:19783652"
FT MUTAGEN 173
FT /note="Y->A: Reduced catalytic activity. Reduces affinity
FT for phosphocholine."
FT /evidence="ECO:0000269|PubMed:19783652"
FT MUTAGEN 362
FT /note="S->A,C: No loss of enzyme activity and nuclear
FT localization."
FT /evidence="ECO:0000269|PubMed:8185307"
FT CONFLICT 91
FT /note="G -> S (in Ref. 1; AAA40995)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="S -> C (in Ref. 1; AAA40995)"
FT /evidence="ECO:0000305"
FT CONFLICT 116..117
FT /note="EL -> DV (in Ref. 2; AAB60489)"
FT /evidence="ECO:0000305"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:3HL4"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:4MVC"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:3HL4"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:4MVC"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:3HL4"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:3HL4"
FT STRAND 102..112
FT /evidence="ECO:0007829|PDB:3HL4"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:3HL4"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:3HL4"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:4MVC"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:3HL4"
FT HELIX 155..160
FT /evidence="ECO:0007829|PDB:3HL4"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:3HL4"
FT HELIX 183..187
FT /evidence="ECO:0007829|PDB:3HL4"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:3HL4"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:3HL4"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:1PEH"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:1PEH"
FT HELIX 248..252
FT /evidence="ECO:0007829|PDB:1PEH"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:1PEH"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:1PEH"
FT HELIX 261..267
FT /evidence="ECO:0007829|PDB:1PEH"
FT HELIX 270..274
FT /evidence="ECO:0007829|PDB:1PEI"
FT HELIX 276..291
FT /evidence="ECO:0007829|PDB:4MVC"
SQ SEQUENCE 367 AA; 41681 MW; 44DFFFC0F1608969 CRC64;
MDAQSSAKVN SRKRRKEVPG PNGATEEDGI PSKVQRCAVG LRQPAPFSDE IEVDFSKPYV
RVTMEEACRG TPCERPVRVY ADGIFDLFHS GHARALMQAK NLFPNTYLIV GVCSDELTHN
FKGFTVMNEN ERYDAVQHCR YVDEVVRNAP WTLTPEFLAE HRIDFVAHDD IPYSSAGSDD
VYKHIKEAGM FAPTQRTEGI STSDIITRIV RDYDVYARRN LQRGYTAKEL NVSFINEKKY
HLQERVDKVK KKVKDVEEKS KEFVQKVEEK SIDLIQKWEE KSREFIGSFL EMFGPEGALK
HMLKEGKGRM LQAISPKQSP SSSPTHERSP SPSFRWPFSG KTSPSSSPAS LSRCKAVTCD
ISEDEED
