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Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PIMT) (EC 2.1.1.77) (L-isoaspartyl protein carboxyl methyltransferase) (Protein L-isoaspartyl/D-aspartyl methyltransferase) (Protein-beta-aspartate methyltransferase)

 PIMT_HUMAN              Reviewed;         227 AA.
P22061; A8K109; J3KP72; Q14661; Q16556; Q5VYC1; Q5VYC2; Q93061;
Q96II9; Q99625; Q9BQV7; Q9BQV8; Q9NP03;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 4.
25-APR-2018, entry version 190.
RecName: Full=Protein-L-isoaspartate(D-aspartate) O-methyltransferase;
Short=PIMT;
EC=2.1.1.77;
AltName: Full=L-isoaspartyl protein carboxyl methyltransferase;
AltName: Full=Protein L-isoaspartyl/D-aspartyl methyltransferase;
AltName: Full=Protein-beta-aspartate methyltransferase;
Name=PCMT1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
PROTEIN SEQUENCE (ISOFORM 1), ACETYLATION AT ALA-2, AND CLEAVAGE OF
INITIATOR METHIONINE.
TISSUE=Erythrocyte;
PubMed=2684970;
Ingrosso D., Fowler A.V., Bleibaum J., Clarke S.;
"Sequence of the D-aspartyl/L-isoaspartyl protein methyltransferase
from human erythrocytes. Common sequence motifs for protein, DNA, RNA,
and small molecule S-adenosylmethionine-dependent
methyltransferases.";
J. Biol. Chem. 264:20131-20139(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT ILE-120.
TISSUE=Brain cortex;
PubMed=1339271; DOI=10.1016/S0006-291X(05)80987-8;
Maclaren D.C., Kagan R.M., Clarke S.;
"Alternative splicing of the human isoaspartyl protein carboxyl
methyltransferase RNA leads to the generation of a C-terminal -RDEL
sequence in isozyme II.";
Biochem. Biophys. Res. Commun. 185:277-283(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
PubMed=7592526; DOI=10.1093/oxfordjournals.jbchem.a124763;
Takeda R., Mizobuchi M., Murao K., Sato M., Takahara J.;
"Characterization of three cDNAs encoding two isozymes of an
isoaspartyl protein carboxyl methyltransferase from human erythroid
leukemia cells.";
J. Biochem. 117:683-685(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Brain;
Shirasawa T., Takahashi H., Endoh R., Sakamoto K., Hirokawa K.,
Mori H.;
"Gene expression of carboxyl methyltransferase is altered in
Alzheimer's disease and the product is localized to neurofibrillary
tangles.";
Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
ILE-120.
TISSUE=Muscle, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
TISSUE=Foreskin;
PubMed=8914929; DOI=10.1006/abbi.1996.0513;
Devry C.G., Tsai W., Clarke S.;
"Structure of the human gene encoding the protein repair L-isoaspartyl
(D-aspartyl) O-methyltransferase.";
Arch. Biochem. Biophys. 335:321-332(1996).
[10]
PROTEIN SEQUENCE OF 5-19; 44-60; 106-170; 179-198 AND 205-220.
PubMed=3167043; DOI=10.1021/bi00414a042;
Gilbert J.M., Fowler A., Bleibaum J., Clarke S.;
"Purification of homologous protein carboxyl methyltransferase
isozymes from human and bovine erythrocytes.";
Biochemistry 27:5227-5233(1988).
[11]
PROTEIN SEQUENCE OF 5-18; 25-37; 82-98; 114-144 AND 179-221, VARIANT
ILE-120, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-53; 100-139 AND 169-224.
PubMed=8074695; DOI=10.1006/bbrc.1994.2209;
Tsai W., Clarke S.;
"Amino acid polymorphisms of the human L-isoaspartyl/D-aspartyl
methyltransferase involved in protein repair.";
Biochem. Biophys. Res. Commun. 203:491-497(1994).
[13]
PARTIAL PROTEIN SEQUENCE (ISOFORM 2), AND VARIANT ILE-120.
TISSUE=Erythrocyte;
PubMed=1998518; DOI=10.1016/S0006-291X(05)81242-2;
Ingrosso D., Kagan R.M., Clarke S.;
"Distinct C-terminal sequences of isozymes I and II of the human
erythrocyte L-isoaspartyl/D-aspartyl protein methyltransferase.";
Biochem. Biophys. Res. Commun. 175:351-358(1991).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[16]
VARIANT ILE-120.
PubMed=10496068; DOI=10.1007/s100380050161;
DeVry C.G., Clarke S.;
"Polymorphic forms of the protein L-isoaspartate (D-aspartate) O-
methyltransferase involved in the repair of age-damaged proteins.";
J. Hum. Genet. 44:275-288(1999).
[17]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
PubMed=11792715; DOI=10.1074/jbc.M200229200;
Ryttersgaard C., Griffith S.C., Sawaya M.R., MacLaren D.C., Clarke S.,
Yeates T.O.;
"Crystal structure of human L-isoaspartyl methyltransferase.";
J. Biol. Chem. 277:10642-10646(2002).
[18]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
PubMed=11847284; DOI=10.1110/ps.37802;
Smith C.D., Carson M., Friedman A.M., Skinner M.M., Delucas L.,
Chantalat L., Weise L., Shirasawa T., Chattopadhyay D.;
"Crystal structure of human L-isoaspartyl-O-methyl-transferase with S-
adenosyl homocysteine at 1.6-A resolution and modeling of an
isoaspartyl-containing peptide at the active site.";
Protein Sci. 11:625-635(2002).
[19]
VARIANT [LARGE SCALE ANALYSIS] ILE-120, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
-!- FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl and
D-aspartyl residues in peptides and proteins that result from
spontaneous decomposition of normal L-aspartyl and L-asparaginyl
residues. It plays a role in the repair and/or degradation of
damaged proteins. Acts on EIF4EBP2, microtubule-associated protein
2, calreticulin, clathrin light chains a and b, Ubiquitin
carboxyl-terminal hydrolase isozyme L1, phosphatidylethanolamine-
binding protein 1, stathmin, beta-synuclein and alpha-synuclein.
{ECO:0000250|UniProtKB:P23506}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + protein L-
isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate
alpha-methyl ester.
-!- SUBUNIT: Monomer.
-!- INTERACTION:
Q13155:AIMP2; NbExp=3; IntAct=EBI-353343, EBI-745226;
P60520:GABARAPL2; NbExp=2; IntAct=EBI-353343, EBI-720116;
P49247:RPIA; NbExp=3; IntAct=EBI-353343, EBI-744831;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P22061-1; Sequence=Displayed;
Name=2;
IsoId=P22061-2; Sequence=VSP_004716;
-!- POLYMORPHISM: The allele frequencies for the polymorphism at codon
120 differ between ethnic groups; in the Caucasian population Ile-
120 is present at a frequency of 0.45, while it is found at a
frequency of 0.88 and 0.81 in the Asian and the African
populations respectively. Val-120 is found at a frequency of 0.55
in the Caucasians, 0.12 and 0.19 in the Asian and African
populations respectively. The Ile-120 variant has higher specific
activity and thermostability than the Val-120 variant. The Val-120
variant has a higher affinity for protein substrates.
-!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
isoaspartyl/D-aspartyl protein methyltransferase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=EAW47786.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; M93008; AAA90934.1; -; mRNA.
EMBL; M93009; AAA90933.1; -; mRNA.
EMBL; D25545; BAA05028.1; -; mRNA.
EMBL; D25546; BAA05029.1; -; mRNA.
EMBL; D25547; BAA05030.1; -; mRNA.
EMBL; D13892; BAA02991.1; -; mRNA.
EMBL; AK289724; BAF82413.1; -; mRNA.
EMBL; AL355312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW47786.1; ALT_SEQ; Genomic_DNA.
EMBL; BC007501; AAH07501.1; -; mRNA.
EMBL; BC008748; AAH08748.1; -; mRNA.
EMBL; U49740; AAB38386.1; -; Genomic_DNA.
EMBL; S73902; AAC60639.2; -; Genomic_DNA.
EMBL; S73903; AAC60640.1; -; Genomic_DNA.
EMBL; S73905; AAC60641.2; -; Genomic_DNA.
PIR; A34489; A34489.
PIR; JH0624; JH0624.
RefSeq; NP_001238978.1; NM_001252049.1.
RefSeq; NP_001238982.1; NM_001252053.1.
RefSeq; NP_005380.2; NM_005389.2.
UniGene; Hs.279257; -.
PDB; 1I1N; X-ray; 1.50 A; A=2-227.
PDB; 1KR5; X-ray; 2.10 A; A=2-227.
PDBsum; 1I1N; -.
PDBsum; 1KR5; -.
ProteinModelPortal; P22061; -.
SMR; P22061; -.
BioGrid; 111141; 112.
IntAct; P22061; 36.
MINT; P22061; -.
STRING; 9606.ENSP00000356348; -.
BindingDB; P22061; -.
ChEMBL; CHEMBL4240; -.
DrugBank; DB01752; S-Adenosyl-L-Homocysteine.
iPTMnet; P22061; -.
PhosphoSitePlus; P22061; -.
BioMuta; PCMT1; -.
DMDM; 317373537; -.
OGP; P22061; -.
REPRODUCTION-2DPAGE; IPI00411680; -.
UCD-2DPAGE; P22061; -.
EPD; P22061; -.
MaxQB; P22061; -.
PaxDb; P22061; -.
PeptideAtlas; P22061; -.
PRIDE; P22061; -.
Ensembl; ENST00000367380; ENSP00000356350; ENSG00000120265.
GeneID; 5110; -.
KEGG; hsa:5110; -.
UCSC; uc011eeg.3; human. [P22061-1]
CTD; 5110; -.
DisGeNET; 5110; -.
EuPathDB; HostDB:ENSG00000120265.16; -.
GeneCards; PCMT1; -.
HGNC; HGNC:8728; PCMT1.
HPA; HPA003239; -.
MIM; 176851; gene.
neXtProt; NX_P22061; -.
eggNOG; KOG1661; Eukaryota.
eggNOG; COG2518; LUCA.
HOVERGEN; HBG004483; -.
InParanoid; P22061; -.
KO; K00573; -.
PhylomeDB; P22061; -.
TreeFam; TF314431; -.
BioCyc; MetaCyc:HS04385-MONOMER; -.
BRENDA; 2.1.1.77; 2681.
Reactome; R-HSA-5676934; Protein repair.
EvolutionaryTrace; P22061; -.
GeneWiki; PCMT1; -.
GenomeRNAi; 5110; -.
PRO; PR:P22061; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000120265; -.
ExpressionAtlas; P22061; baseline and differential.
Genevisible; P22061; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; TAS:UniProtKB.
GO; GO:0006479; P:protein methylation; TAS:ProtInc.
GO; GO:0030091; P:protein repair; TAS:UniProtKB.
InterPro; IPR000682; PCMT.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR11579; PTHR11579; 1.
SUPFAM; SSF53335; SSF53335; 1.
TIGRFAMs; TIGR00080; pimt; 1.
PROSITE; PS01279; PCMT; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Disulfide bond;
Methyltransferase; Polymorphism; Reference proteome;
S-adenosyl-L-methionine; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2684970}.
CHAIN 2 227 Protein-L-isoaspartate(D-aspartate) O-
methyltransferase.
/FTId=PRO_0000111875.
ACT_SITE 60 60
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:2684970}.
DISULFID 43 95 {ECO:0000250}.
VAR_SEQ 226 227 WK -> DEL (in isoform 2).
{ECO:0000303|PubMed:1339271,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7592526,
ECO:0000303|Ref.4}.
/FTId=VSP_004716.
VARIANT 120 120 V -> I (in dbSNP:rs4816).
{ECO:0000244|PubMed:21269460,
ECO:0000269|PubMed:10496068,
ECO:0000269|PubMed:1339271,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1998518,
ECO:0000269|Ref.11}.
/FTId=VAR_006173.
CONFLICT 19 19 K -> G (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 23 23 I -> L (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 60 60 S -> A (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 102 102 C -> Q (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 168 168 A -> P (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 206 206 K -> R (in Ref. 2; AAA90933).
{ECO:0000305}.
HELIX 10 19 {ECO:0000244|PDB:1I1N}.
HELIX 26 33 {ECO:0000244|PDB:1I1N}.
HELIX 37 39 {ECO:0000244|PDB:1I1N}.
STRAND 47 49 {ECO:0000244|PDB:1I1N}.
STRAND 51 54 {ECO:0000244|PDB:1I1N}.
STRAND 57 59 {ECO:0000244|PDB:1I1N}.
HELIX 62 71 {ECO:0000244|PDB:1I1N}.
TURN 72 75 {ECO:0000244|PDB:1I1N}.
STRAND 81 85 {ECO:0000244|PDB:1I1N}.
HELIX 91 100 {ECO:0000244|PDB:1I1N}.
TURN 101 103 {ECO:0000244|PDB:1KR5}.
STRAND 105 111 {ECO:0000244|PDB:1I1N}.
HELIX 113 126 {ECO:0000244|PDB:1I1N}.
HELIX 129 132 {ECO:0000244|PDB:1I1N}.
STRAND 134 141 {ECO:0000244|PDB:1I1N}.
HELIX 143 145 {ECO:0000244|PDB:1I1N}.
HELIX 148 150 {ECO:0000244|PDB:1I1N}.
STRAND 153 158 {ECO:0000244|PDB:1I1N}.
STRAND 160 164 {ECO:0000244|PDB:1I1N}.
HELIX 167 171 {ECO:0000244|PDB:1I1N}.
STRAND 173 184 {ECO:0000244|PDB:1I1N}.
STRAND 190 197 {ECO:0000244|PDB:1I1N}.
STRAND 203 211 {ECO:0000244|PDB:1I1N}.
HELIX 219 222 {ECO:0000244|PDB:1I1N}.
SEQUENCE 227 AA; 24636 MW; 4EB1122379C8040A CRC64;
MAWKSGGASH SELIHNLRKN GIIKTDKVFE VMLATDRSHY AKCNPYMDSP QSIGFQATIS
APHMHAYALE LLFDQLHEGA KALDVGSGSG ILTACFARMV GCTGKVIGID HIKELVDDSV
NNVRKDDPTL LSSGRVQLVV GDGRMGYAEE APYDAIHVGA AAPVVPQALI DQLKPGGRLI
LPVGPAGGNQ MLEQYDKLQD GSIKMKPLMG VIYVPLTDKE KQWSRWK


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