MYP2_HUMAN
ID MYP2_HUMAN Reviewed; 132 AA.
AC P02689; Q6FHL4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Myelin P2 protein;
DE AltName: Full=Peripheral myelin protein 2;
GN Name=PMP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1720307; DOI=10.1016/s0006-291x(05)81402-0;
RA Hayasaka K., Nanao K., Tahara M., Sato W., Takada G., Miura M., Uyemura K.;
RT "Isolation and sequence determination of cDNA encoding P2 protein of human
RT peripheral myelin.";
RL Biochem. Biophys. Res. Commun. 181:204-207(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-116.
RX PubMed=7525873; DOI=10.1046/j.1471-4159.1994.63062010.x;
RA Narayanan V., Ripepi B., Jabs E.W., Hawkins A., Griffin C., Tennekoon G.;
RT "Partial structure and mapping of the human myelin P2 protein gene.";
RL J. Neurochem. 63:2010-2013(1994).
RN [8]
RP PROTEIN SEQUENCE OF 2-132, AND ACETYLATION AT SER-2.
RX PubMed=6183401; DOI=10.1111/j.1471-4159.1982.tb08017.x;
RA Suzuki M., Kitamura K., Sakamoto Y., Uyemura K.;
RT "The complete amino acid sequence of human P2 protein.";
RL J. Neurochem. 39:1759-1762(1982).
RN [9] {ECO:0007744|PDB:2WUT}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH PALMITATE, FUNCTION,
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, CIRCULAR DICHROISM, AND
RP DOMAIN.
RX PubMed=20421974; DOI=10.1371/journal.pone.0010300;
RA Majava V., Polverini E., Mazzini A., Nanekar R., Knoll W., Peters J.,
RA Natali F., Baumgartel P., Kursula I., Kursula P.;
RT "Structural and functional characterization of human peripheral nervous
RT system myelin protein P2.";
RL PLoS ONE 5:E10300-E10300(2010).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 3-132.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human peripheral myelin protein 2.";
RL Submitted (AUG-2010) to the PDB data bank.
RN [11]
RP VARIANT CMT1G ASN-43, AND INVOLVEMENT IN CMT1G.
RX PubMed=26257172; DOI=10.1016/j.celrep.2015.07.023;
RG Baylor-Hopkins Center for Mendelian Genomics;
RA Gonzaga-Jauregui C., Harel T., Gambin T., Kousi M., Griffin L.B.,
RA Francescatto L., Ozes B., Karaca E., Jhangiani S.N., Bainbridge M.N.,
RA Lawson K.S., Pehlivan D., Okamoto Y., Withers M., Mancias P.,
RA Slavotinek A., Reitnauer P.J., Goksungur M.T., Shy M., Crawford T.O.,
RA Koenig M., Willer J., Flores B.N., Pediaditrakis I., Us O., Wiszniewski W.,
RA Parman Y., Antonellis A., Muzny D.M., Katsanis N., Battaloglu E.,
RA Boerwinkle E., Gibbs R.A., Lupski J.R.;
RT "Exome sequence analysis suggests that genetic burden contributes to
RT phenotypic variability and complex neuropathy.";
RL Cell Rep. 12:1169-1183(2015).
RN [12]
RP VARIANTS CMT1G PRO-51 AND THR-52, AND INVOLVEMENT IN CMT1G.
RX PubMed=27009151; DOI=10.1093/brain/aww055;
RA Motley W.W., Palaima P., Yum S.W., Gonzalez M.A., Tao F., Wanschitz J.V.,
RA Strickland A.V., Loescher W.N., De Vriendt E., Koppi S., Medne L.,
RA Janecke A.R., Jordanova A., Zuchner S., Scherer S.S.;
RT "De novo PMP2 mutations in families with type 1 Charcot-Marie-Tooth
RT disease.";
RL Brain 139:1649-1656(2016).
RN [13]
RP VARIANT CMT1G ASN-43, AND INVOLVEMENT IN CMT1G.
RX PubMed=26828946; DOI=10.1371/journal.pgen.1005829;
RA Hong Y.B., Joo J., Hyun Y.S., Kwak G., Choi Y.R., Yeo H.K., Jwa D.H.,
RA Kim E.J., Mo W.M., Nam S.H., Kim S.M., Yoo J.H., Koo H., Park H.T.,
RA Chung K.W., Choi B.O.;
RT "A mutation in PMP2 causes dominant demyelinating Charcot-Marie-Tooth
RT neuropathy.";
RL PLoS Genet. 12:E1005829-E1005829(2016).
RN [14]
RP VARIANT CMT1G THR-52, AND INVOLVEMENT IN CMT1G.
RX PubMed=30249361; DOI=10.1016/j.ymgme.2018.08.005;
RA Punetha J., Mackay-Loder L., Harel T., Coban-Akdemir Z., Jhangiani S.N.,
RA Gibbs R.A., Lee I., Terespolsky D., Lupski J.R., Posey J.E.;
RT "Identification of a pathogenic PMP2 variant in a multi-generational family
RT with CMT type 1: Clinical gene panels versus genome-wide approaches to
RT molecular diagnosis.";
RL Mol. Genet. Metab. 125:302-304(2018).
CC -!- FUNCTION: May play a role in lipid transport protein in Schwann cells.
CC May bind cholesterol. {ECO:0000269|PubMed:20421974}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20421974}.
CC -!- INTERACTION:
CC P02689; O95273: CCNDBP1; NbExp=4; IntAct=EBI-10193858, EBI-748961;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior. {ECO:0000269|PubMed:20421974}.
CC -!- DISEASE: Charcot-Marie-Tooth disease, demyelinating, 1G (CMT1G)
CC [MIM:618279]: An autosomal dominant demyelinating form of Charcot-
CC Marie-Tooth disease, a disorder of the peripheral nervous system,
CC characterized by progressive weakness and atrophy, initially of the
CC peroneal muscles and later of the distal muscles of the arms. Charcot-
CC Marie-Tooth disease is classified in two main groups on the basis of
CC electrophysiologic properties and histopathology: primary peripheral
CC demyelinating neuropathies (designated CMT1 when they are dominantly
CC inherited) and primary peripheral axonal neuropathies (CMT2).
CC Demyelinating neuropathies are characterized by severely reduced nerve
CC conduction velocities (less than 38 m/sec), segmental demyelination and
CC remyelination with onion bulb formations on nerve biopsy, slowly
CC progressive distal muscle atrophy and weakness, absent deep tendon
CC reflexes, and hollow feet. CMT1G is characterized by distal muscle
CC weakness and atrophy with onset in the first or second decade.
CC {ECO:0000269|PubMed:26257172, ECO:0000269|PubMed:26828946,
CC ECO:0000269|PubMed:27009151, ECO:0000269|PubMed:30249361}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: P2 protein and myelin basic protein together constitute
CC a major fraction of peripheral nervous system myelin protein.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; D16181; BAA03726.1; -; Genomic_DNA.
DR EMBL; X62167; CAA44096.1; -; mRNA.
DR EMBL; AK311758; BAG34701.1; -; mRNA.
DR EMBL; CR541649; CAG46450.1; -; mRNA.
DR EMBL; CR541738; CAG46538.1; -; mRNA.
DR EMBL; AC018616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471068; EAW87090.1; -; Genomic_DNA.
DR EMBL; BC034997; AAH34997.1; -; mRNA.
DR EMBL; AH004648; AAB32592.2; -; Genomic_DNA.
DR CCDS; CCDS6229.1; -.
DR PIR; JT0977; MPHU2.
DR RefSeq; NP_002668.1; NM_002677.4.
DR PDB; 2WUT; X-ray; 1.85 A; A=1-132.
DR PDB; 3NR3; X-ray; 1.95 A; A=3-132.
DR PDB; 4A1H; X-ray; 2.20 A; A/B/C=1-132.
DR PDB; 4A1Y; X-ray; 1.20 A; A/B/C/D=1-132.
DR PDB; 4A8Z; X-ray; 1.80 A; A=1-132.
DR PDB; 4BVM; X-ray; 0.93 A; A=1-132.
DR PDB; 4D6A; X-ray; 1.45 A; A=1-132.
DR PDB; 4D6B; X-ray; 2.12 A; A=1-132.
DR PDB; 5N4M; X-ray; 1.59 A; A=1-132.
DR PDB; 5N4P; X-ray; 1.53 A; A=1-132.
DR PDB; 5N4Q; X-ray; 1.72 A; A=1-132.
DR PDB; 6EW2; X-ray; 1.59 A; A=1-132.
DR PDB; 6EW4; X-ray; 1.27 A; A=1-132.
DR PDB; 6EW5; X-ray; 1.95 A; A/B/C/D=1-132.
DR PDB; 6S2M; X-ray; 0.72 A; A=1-132.
DR PDB; 6S2S; X-ray; 0.86 A; A=1-132.
DR PDB; 6STS; X-ray; 3.00 A; A/B=1-132.
DR PDB; 6XU5; X-ray; 1.65 A; A=1-132.
DR PDB; 6XU9; X-ray; 2.70 A; A=1-132.
DR PDB; 6XUA; X-ray; 2.30 A; B=1-132.
DR PDB; 6XUW; X-ray; 2.31 A; A=1-132.
DR PDB; 6XVQ; X-ray; 1.80 A; A=1-132.
DR PDB; 6XVR; X-ray; 2.00 A; A=1-132.
DR PDB; 6XVS; X-ray; 1.80 A; A/B=1-132.
DR PDB; 6XVY; X-ray; 1.80 A; B/C/D/E=1-132.
DR PDB; 6XW9; X-ray; 2.90 A; A=1-132.
DR PDB; 7NRW; X-ray; 2.00 A; A=1-132.
DR PDB; 7NSR; X-ray; 1.50 A; A=1-132.
DR PDB; 7NTP; X-ray; 2.10 A; A/B=1-132.
DR PDB; 7O60; Other; 2.00 A; A=1-132.
DR PDBsum; 2WUT; -.
DR PDBsum; 3NR3; -.
DR PDBsum; 4A1H; -.
DR PDBsum; 4A1Y; -.
DR PDBsum; 4A8Z; -.
DR PDBsum; 4BVM; -.
DR PDBsum; 4D6A; -.
DR PDBsum; 4D6B; -.
DR PDBsum; 5N4M; -.
DR PDBsum; 5N4P; -.
DR PDBsum; 5N4Q; -.
DR PDBsum; 6EW2; -.
DR PDBsum; 6EW4; -.
DR PDBsum; 6EW5; -.
DR PDBsum; 6S2M; -.
DR PDBsum; 6S2S; -.
DR PDBsum; 6STS; -.
DR PDBsum; 6XU5; -.
DR PDBsum; 6XU9; -.
DR PDBsum; 6XUA; -.
DR PDBsum; 6XUW; -.
DR PDBsum; 6XVQ; -.
DR PDBsum; 6XVR; -.
DR PDBsum; 6XVS; -.
DR PDBsum; 6XVY; -.
DR PDBsum; 6XW9; -.
DR PDBsum; 7NRW; -.
DR PDBsum; 7NSR; -.
DR PDBsum; 7NTP; -.
DR PDBsum; 7O60; -.
DR AlphaFoldDB; P02689; -.
DR SASBDB; P02689; -.
DR SMR; P02689; -.
DR BioGRID; 111388; 9.
DR IntAct; P02689; 3.
DR STRING; 9606.ENSP00000256103; -.
DR ChEMBL; CHEMBL3826864; -.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR DrugBank; DB04224; Oleic Acid.
DR DrugBank; DB03796; Palmitic Acid.
DR DrugBank; DB01915; S-Hydroxycysteine.
DR iPTMnet; P02689; -.
DR PhosphoSitePlus; P02689; -.
DR SwissPalm; P02689; -.
DR BioMuta; PMP2; -.
DR DMDM; 127725; -.
DR jPOST; P02689; -.
DR MassIVE; P02689; -.
DR MaxQB; P02689; -.
DR PaxDb; P02689; -.
DR PeptideAtlas; P02689; -.
DR PRIDE; P02689; -.
DR ProteomicsDB; 51553; -.
DR Antibodypedia; 25321; 176 antibodies from 22 providers.
DR DNASU; 5375; -.
DR Ensembl; ENST00000256103.3; ENSP00000256103.2; ENSG00000147588.7.
DR GeneID; 5375; -.
DR KEGG; hsa:5375; -.
DR MANE-Select; ENST00000256103.3; ENSP00000256103.2; NM_002677.5; NP_002668.1.
DR UCSC; uc003ycb.3; human.
DR CTD; 5375; -.
DR DisGeNET; 5375; -.
DR GeneCards; PMP2; -.
DR HGNC; HGNC:9117; PMP2.
DR HPA; ENSG00000147588; Group enriched (brain, choroid plexus).
DR MalaCards; PMP2; -.
DR MIM; 170715; gene.
DR MIM; 618279; phenotype.
DR neXtProt; NX_P02689; -.
DR OpenTargets; ENSG00000147588; -.
DR Orphanet; 476394; PMP2-related Charcot-Marie-Tooth disease type 1.
DR PharmGKB; PA33443; -.
DR VEuPathDB; HostDB:ENSG00000147588; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000160445; -.
DR HOGENOM; CLU_113772_0_0_1; -.
DR InParanoid; P02689; -.
DR OMA; CIMGDVI; -.
DR OrthoDB; 1417203at2759; -.
DR PhylomeDB; P02689; -.
DR TreeFam; TF316894; -.
DR PathwayCommons; P02689; -.
DR SignaLink; P02689; -.
DR BioGRID-ORCS; 5375; 10 hits in 1063 CRISPR screens.
DR ChiTaRS; PMP2; human.
DR EvolutionaryTrace; P02689; -.
DR GeneWiki; PMP2; -.
DR GenomeRNAi; 5375; -.
DR Pharos; P02689; Tbio.
DR PRO; PR:P02689; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P02689; protein.
DR Bgee; ENSG00000147588; Expressed in olfactory bulb and 150 other tissues.
DR ExpressionAtlas; P02689; baseline and differential.
DR Genevisible; P02689; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0043209; C:myelin sheath; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; IDA:UniProtKB.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0061024; P:membrane organization; IEA:Ensembl.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR InterPro; IPR031256; Myelin_P2.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR PANTHER; PTHR11955:SF64; PTHR11955:SF64; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00214; FABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Charcot-Marie-Tooth disease; Cytoplasm;
KW Direct protein sequencing; Disease variant; Disulfide bond; Lipid-binding;
KW Neurodegeneration; Neuropathy; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6183401"
FT CHAIN 2..132
FT /note="Myelin P2 protein"
FT /id="PRO_0000067388"
FT BINDING 107
FT /ligand="(9Z)-octadecenoate"
FT /ligand_id="ChEBI:CHEBI:30823"
FT /evidence="ECO:0000250|UniProtKB:P02690"
FT BINDING 107
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:20421974,
FT ECO:0007744|PDB:2WUT"
FT BINDING 127..129
FT /ligand="(9Z)-octadecenoate"
FT /ligand_id="ChEBI:CHEBI:30823"
FT /evidence="ECO:0000250|UniProtKB:P02690"
FT BINDING 127..129
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:20421974,
FT ECO:0007744|PDB:2WUT"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:6183401"
FT DISULFID 118..125
FT /evidence="ECO:0000269|PubMed:6183401"
FT VARIANT 43
FT /note="I -> N (in CMT1G; dbSNP:rs879253869)"
FT /evidence="ECO:0000269|PubMed:26257172,
FT ECO:0000269|PubMed:26828946"
FT /id="VAR_081897"
FT VARIANT 51
FT /note="T -> P (in CMT1G; dbSNP:rs1563518390)"
FT /evidence="ECO:0000269|PubMed:27009151"
FT /id="VAR_081898"
FT VARIANT 52
FT /note="I -> T (in CMT1G; dbSNP:rs1563518388)"
FT /evidence="ECO:0000269|PubMed:27009151,
FT ECO:0000269|PubMed:30249361"
FT /id="VAR_081899"
FT CONFLICT 25
FT /note="G -> GG (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="D -> N (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="N -> D (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:6S2M"
FT STRAND 7..16
FT /evidence="ECO:0007829|PDB:6S2M"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:6S2M"
FT HELIX 28..36
FT /evidence="ECO:0007829|PDB:6S2M"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:6S2M"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:6S2M"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:6S2M"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:6S2M"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:6S2M"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:6S2M"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:6S2M"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:6S2M"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:6S2M"
SQ SEQUENCE 132 AA; 14909 MW; 3D515D32695899D2 CRC64;
MSNKFLGTWK LVSSENFDDY MKALGVGLAT RKLGNLAKPT VIISKKGDII TIRTESTFKN
TEISFKLGQE FEETTADNRK TKSIVTLQRG SLNQVQRWDG KETTIKRKLV NGKMVAECKM
KGVVCTRIYE KV
