MYP2_BOVIN
ID MYP2_BOVIN Reviewed; 132 AA.
AC P02690; Q0VCJ4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Myelin P2 protein;
GN Name=PMP2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-132, AND ACETYLATION AT SER-2.
RX PubMed=6156092; DOI=10.1016/0014-5793(80)80719-8;
RA Kitamura K., Suzuki M., Suzuki A., Uyemura K.;
RT "The complete amino acid sequence of the P2 protein in bovine peripheral
RT nerve myelin.";
RL FEBS Lett. 115:27-30(1980).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=2458918; DOI=10.1002/j.1460-2075.1988.tb02985.x;
RA Jones T.A., Bergfors T., Sedzik J., Unge T.;
RT "The three-dimensional structure of P2 myelin protein.";
RL EMBO J. 7:1597-1604(1988).
RN [4] {ECO:0007744|PDB:1PMP}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH OLEATE.
RX PubMed=7683727; DOI=10.1006/jmbi.1993.1238;
RA Cowan S.W., Newcomer M.E., Jones T.A.;
RT "Crystallographic studies on a family of cellular lipophilic transport
RT proteins. Refinement of P2 myelin protein and the structure determination
RT and refinement of cellular retinol-binding protein in complex with all-
RT trans-retinol.";
RL J. Mol. Biol. 230:1225-1246(1993).
CC -!- FUNCTION: May play a role in lipid transport protein in Schwann cells.
CC May bind cholesterol.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7683727}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior.
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; BC120137; AAI20138.1; -; mRNA.
DR PIR; A03144; MPBO2.
DR RefSeq; NP_001068707.1; NM_001075239.2.
DR PDB; 1PMP; X-ray; 2.70 A; A/B/C=2-132.
DR PDBsum; 1PMP; -.
DR AlphaFoldDB; P02690; -.
DR SMR; P02690; -.
DR STRING; 9913.ENSBTAP00000043814; -.
DR iPTMnet; P02690; -.
DR PaxDb; P02690; -.
DR PeptideAtlas; P02690; -.
DR PRIDE; P02690; -.
DR Ensembl; ENSBTAT00000046521; ENSBTAP00000043814; ENSBTAG00000000071.
DR GeneID; 506062; -.
DR KEGG; bta:506062; -.
DR CTD; 5375; -.
DR VEuPathDB; HostDB:ENSBTAG00000000071; -.
DR VGNC; VGNC:53876; PMP2.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000160445; -.
DR HOGENOM; CLU_113772_0_0_1; -.
DR InParanoid; P02690; -.
DR OMA; CIMGDVI; -.
DR OrthoDB; 1417203at2759; -.
DR TreeFam; TF316894; -.
DR EvolutionaryTrace; P02690; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000000071; Expressed in intramuscular adipose tissue and 36 other tissues.
DR ExpressionAtlas; P02690; baseline.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; ISS: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; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Lipid-binding; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6156092"
FT CHAIN 2..132
FT /note="Myelin P2 protein"
FT /id="PRO_0000067387"
FT BINDING 107
FT /ligand="(9Z)-octadecenoate"
FT /ligand_id="ChEBI:CHEBI:30823"
FT /evidence="ECO:0000269|PubMed:7683727,
FT ECO:0007744|PDB:1PMP"
FT BINDING 107
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000250|UniProtKB:P02689"
FT BINDING 127..129
FT /ligand="(9Z)-octadecenoate"
FT /ligand_id="ChEBI:CHEBI:30823"
FT /evidence="ECO:0000269|PubMed:7683727,
FT ECO:0007744|PDB:1PMP"
FT BINDING 127..129
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000250|UniProtKB:P02689"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:6156092"
FT DISULFID 118..125
FT /evidence="ECO:0000269|PubMed:6156092"
FT CONFLICT 99
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:1PMP"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:1PMP"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:1PMP"
FT HELIX 28..35
FT /evidence="ECO:0007829|PDB:1PMP"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:1PMP"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:1PMP"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:1PMP"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:1PMP"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:1PMP"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:1PMP"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:1PMP"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:1PMP"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:1PMP"
SQ SEQUENCE 132 AA; 14950 MW; 14759D2AAF8CFB21 CRC64;
MSNKFLGTWK LVSSENFDEY MKALGVGLAT RKLGNLAKPR VIISKKGDII TIRTESPFKN
TEISFKLGQE FEETTADNRK TKSTVTLARG SLNQVQKWDG NETTIKRKLV DGKMVVECKM
KDVVCTRIYE KV
