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Database: UniProt
Entry: P17535
LinkDB: P17535
Original site: P17535 
ID   JUND_HUMAN              Reviewed;         347 AA.
AC   P17535; Q53EK9;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 3.
DT   02-JUN-2021, entry version 195.
DE   RecName: Full=Transcription factor jun-D;
GN   Name=JUND;
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=1903194;
RA   Berger I., Shaul Y.;
RT   "Structure and function of human jun-D.";
RL   Oncogene 6:561-566(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-20.
RG   NIEHS SNPs program;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 45-347.
RX   PubMed=2112242; DOI=10.1093/nar/18.10.3047;
RA   Nomura N., Ide M., Sasamoto S., Matsui M., Date T., Ishizaki R.;
RT   "Isolation of human cDNA clones of jun-related genes, jun-B and jun-D.";
RL   Nucleic Acids Res. 18:3047-3048(1990).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH MEN1.
RX   PubMed=9989505; DOI=10.1016/s0092-8674(00)80967-8;
RA   Agarwal S.K., Guru S.C., Heppner C., Erdos M.R., Collins R.M., Park S.Y.,
RA   Saggar S., Chandrasekharappa S.C., Collins F.S., Spiegel A.M., Marx S.J.,
RA   Burns A.L.;
RT   "Menin interacts with the AP1 transcription factor JunD and represses JunD-
RT   activated transcription.";
RL   Cell 96:143-152(1999).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251; SER-255 AND SER-259, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-259, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-259, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [12] {ECO:0007744|PDB:3U86}
RP   X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS) OF 27-39 IN COMPLEX WITH MEN1,
RP   INTERACTION WITH MEN1 AND MAPK10, DOMAIN MENIN-BINDING AND MAP KINASE
RP   DOCKING MOTIFS, MUTAGENESIS OF ARG-30; LEU-31; PHE-32; PRO-33; GLY-34;
RP   ALA-35; PRO-36; PRO-37; LYS-46; LYS-47; LEU-52 AND LEU-54, AND
RP   PHOSPHORYLATION AT SER-90; SER-100 AND THR-117.
RX   PubMed=22327296; DOI=10.1038/nature10806;
RA   Huang J., Gurung B., Wan B., Matkar S., Veniaminova N.A., Wan K.,
RA   Merchant J.L., Hua X., Lei M.;
RT   "The same pocket in menin binds both MLL and JUND but has opposite effects
RT   on transcription.";
RL   Nature 482:542-546(2012).
CC   -!- FUNCTION: Transcription factor binding AP-1 sites.
CC       {ECO:0000269|PubMed:9989505}.
CC   -!- SUBUNIT: Binds DNA as a dimer (By similarity). Interacts (via MBM
CC       motif) with MEN1; this interaction represses transcriptional activation
CC       (PubMed:9989505, PubMed:22327296). Interacts with MAPK10; this
CC       interaction is inhibited in the presence of MEN1 (PubMed:22327296).
CC       {ECO:0000250, ECO:0000269|PubMed:22327296, ECO:0000269|PubMed:9989505}.
CC   -!- INTERACTION:
CC       P17535; P61158: ACTR3; NbExp=2; IntAct=EBI-2682803, EBI-351428;
CC       P17535; P05067: APP; NbExp=3; IntAct=EBI-2682803, EBI-77613;
CC       P17535; P15336: ATF2; NbExp=3; IntAct=EBI-2682803, EBI-1170906;
CC       P17535; P18847: ATF3; NbExp=3; IntAct=EBI-2682803, EBI-712767;
CC       P17535; P17544: ATF7; NbExp=2; IntAct=EBI-2682803, EBI-765623;
CC       P17535; Q16520: BATF; NbExp=2; IntAct=EBI-2682803, EBI-749503;
CC       P17535; Q9NR55: BATF3; NbExp=3; IntAct=EBI-2682803, EBI-10312707;
CC       P17535; P01100: FOS; NbExp=10; IntAct=EBI-2682803, EBI-852851;
CC       P17535; P15408: FOSL2; NbExp=4; IntAct=EBI-2682803, EBI-3893419;
CC       P17535; P53779: MAPK10; NbExp=2; IntAct=EBI-2682803, EBI-713543;
CC       P17535; Q00987: MDM2; NbExp=3; IntAct=EBI-2682803, EBI-389668;
CC       P17535; O00255-2: MEN1; NbExp=6; IntAct=EBI-2682803, EBI-9869387;
CC       P17535; P0C746: HBZ; Xeno; NbExp=2; IntAct=EBI-2682803, EBI-10890294;
CC       P17535; Q9DGW5: MDV005; Xeno; NbExp=2; IntAct=EBI-2682803, EBI-10889526;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: Phosphorylated by MAP kinases MAPK8 and MAPK10; phosphorylation is
CC       inhibited in the presence of MEN1. {ECO:0000269|PubMed:22327296}.
CC   -!- SIMILARITY: Belongs to the bZIP family. Jun subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA40010.1; Type=Frameshift; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/tnfrsf1b/";
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/JUNDID179.html";
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DR   EMBL; X56681; CAA40010.1; ALT_FRAME; mRNA.
DR   EMBL; EF044249; ABJ53425.1; -; Genomic_DNA.
DR   EMBL; AK223630; BAD97350.1; -; mRNA.
DR   EMBL; CH471106; EAW84684.1; -; Genomic_DNA.
DR   EMBL; X51346; CAA35739.1; -; mRNA.
DR   CCDS; CCDS32959.1; -.
DR   PIR; A43815; A43815.
DR   PIR; S10184; TVHUJD.
DR   RefSeq; NP_001273897.1; NM_001286968.1.
DR   RefSeq; NP_005345.3; NM_005354.5.
DR   PDB; 3U86; X-ray; 2.84 A; B=27-39.
DR   PDB; 5VPA; X-ray; 2.83 A; B=266-332.
DR   PDB; 5VPB; X-ray; 2.69 A; B/D=266-332.
DR   PDB; 5VPC; X-ray; 2.50 A; B/D=266-332.
DR   PDB; 5VPD; X-ray; 2.79 A; B/D=266-332.
DR   PDB; 5VPE; X-ray; 2.05 A; B/D=266-332.
DR   PDB; 5VPF; X-ray; 2.69 A; B/D=266-332.
DR   PDBsum; 3U86; -.
DR   PDBsum; 5VPA; -.
DR   PDBsum; 5VPB; -.
DR   PDBsum; 5VPC; -.
DR   PDBsum; 5VPD; -.
DR   PDBsum; 5VPE; -.
DR   PDBsum; 5VPF; -.
DR   SMR; P17535; -.
DR   BioGRID; 109930; 55.
DR   ComplexPortal; CPX-497; Menin-JUND transcription inhibition complex.
DR   CORUM; P17535; -.
DR   DIP; DIP-1053N; -.
DR   IntAct; P17535; 36.
DR   MINT; P17535; -.
DR   STRING; 9606.ENSP00000252818; -.
DR   GlyGen; P17535; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P17535; -.
DR   PhosphoSitePlus; P17535; -.
DR   BioMuta; JUND; -.
DR   DMDM; 229462969; -.
DR   EPD; P17535; -.
DR   jPOST; P17535; -.
DR   MassIVE; P17535; -.
DR   MaxQB; P17535; -.
DR   PaxDb; P17535; -.
DR   PeptideAtlas; P17535; -.
DR   PRIDE; P17535; -.
DR   ProteomicsDB; 53481; -.
DR   Antibodypedia; 3936; 645 antibodies.
DR   DNASU; 3727; -.
DR   Ensembl; ENST00000252818; ENSP00000252818; ENSG00000130522.
DR   GeneID; 3727; -.
DR   KEGG; hsa:3727; -.
DR   UCSC; uc002nip.4; human.
DR   CTD; 3727; -.
DR   DisGeNET; 3727; -.
DR   GeneCards; JUND; -.
DR   HGNC; HGNC:6206; JUND.
DR   HPA; ENSG00000130522; Tissue enhanced (bone).
DR   MIM; 165162; gene.
DR   neXtProt; NX_P17535; -.
DR   OpenTargets; ENSG00000130522; -.
DR   PharmGKB; PA30008; -.
DR   VEuPathDB; HostDB:ENSG00000130522.5; -.
DR   eggNOG; KOG0837; Eukaryota.
DR   GeneTree; ENSGT00940000162806; -.
DR   HOGENOM; CLU_057007_0_0_1; -.
DR   InParanoid; P17535; -.
DR   OMA; PHEVQVH; -.
DR   OrthoDB; 1090460at2759; -.
DR   PhylomeDB; P17535; -.
DR   TreeFam; TF323952; -.
DR   PathwayCommons; P17535; -.
DR   Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR   Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR   SignaLink; P17535; -.
DR   SIGNOR; P17535; -.
DR   BioGRID-ORCS; 3727; 18 hits in 1015 CRISPR screens.
DR   ChiTaRS; JUND; human.
DR   GeneWiki; JunD; -.
DR   GenomeRNAi; 3727; -.
DR   Pharos; P17535; Tbio.
DR   PRO; PR:P17535; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P17535; protein.
DR   Bgee; ENSG00000130522; Expressed in mammary gland and 260 other tissues.
DR   ExpressionAtlas; P17535; baseline and differential.
DR   Genevisible; P17535; HS.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0032993; C:protein-DNA complex; IEA:Ensembl.
DR   GO; GO:0035976; C:transcription factor AP-1 complex; IDA:CAFA.
DR   GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0016922; F:nuclear receptor binding; IEA:Ensembl.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0008134; F:transcription factor binding; IBA:GO_Central.
DR   GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0007568; P:aging; IEA:Ensembl.
DR   GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
DR   GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR   GO; GO:0002076; P:osteoblast development; IEA:Ensembl.
DR   GO; GO:0043032; P:positive regulation of macrophage activation; IEA:Ensembl.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:CAFA.
DR   GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0009416; P:response to light stimulus; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR   GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR   IDEAL; IID00542; -.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR005643; JNK.
DR   InterPro; IPR029823; JunD.
DR   InterPro; IPR002112; Leuzip_Jun.
DR   InterPro; IPR008917; TF_DNA-bd_sf.
DR   PANTHER; PTHR11462:SF7; PTHR11462:SF7; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   Pfam; PF03957; Jun; 1.
DR   PRINTS; PR00043; LEUZIPPRJUN.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF47454; SSF47454; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..347
FT                   /note="Transcription factor jun-D"
FT                   /id="PRO_0000076442"
FT   DOMAIN          268..331
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          62..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          268..295
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          296..324
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   MOTIF           27..39
FT                   /note="Menin-binding motif (MBM)"
FT                   /evidence="ECO:0000269|PubMed:22327296"
FT   MOTIF           46..55
FT                   /note="MAP kinase docking motif; essential for its
FT                   phosphorylation"
FT                   /evidence="ECO:0000269|PubMed:22327296"
FT   MOD_RES         90
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:22327296"
FT   MOD_RES         100
FT                   /note="Phosphoserine; by MAPK8"
FT                   /evidence="ECO:0000269|PubMed:22327296"
FT   MOD_RES         117
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:22327296"
FT   MOD_RES         251
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         255
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         259
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231"
FT   VARIANT         20
FT                   /note="G -> V (in dbSNP:rs41478151)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_055247"
FT   MUTAGEN         30
FT                   /note="R->A: Reduced interaction with MEN1."
FT                   /evidence="ECO:0000269|PubMed:22327296"
FT   MUTAGEN         31
FT                   /note="L->A: Reduced interaction with MEN1."
FT                   /evidence="ECO:0000269|PubMed:22327296"
FT   MUTAGEN         32
FT                   /note="F->A: Loss of interaction with MEN1."
FT                   /evidence="ECO:0000269|PubMed:22327296"
FT   MUTAGEN         33
FT                   /note="P->A: Loss of interaction with MEN1."
FT                   /evidence="ECO:0000269|PubMed:22327296"
FT   MUTAGEN         34
FT                   /note="G->R: Loss of interaction with MEN1."
FT                   /evidence="ECO:0000269|PubMed:22327296"
FT   MUTAGEN         35
FT                   /note="A->R: Reduced interaction with MEN1."
FT                   /evidence="ECO:0000269|PubMed:22327296"
FT   MUTAGEN         36
FT                   /note="P->A: Reduced interaction with MEN1."
FT                   /evidence="ECO:0000269|PubMed:22327296"
FT   MUTAGEN         37
FT                   /note="P->A: Reduced interaction with MEN1."
FT                   /evidence="ECO:0000269|PubMed:22327296"
FT   MUTAGEN         46
FT                   /note="K->A: Loss of phosphorylation; when associated with
FT                   A-47."
FT                   /evidence="ECO:0000269|PubMed:22327296"
FT   MUTAGEN         46
FT                   /note="K->E: Reduced interaction with MEN1; when associated
FT                   with E-47."
FT                   /evidence="ECO:0000269|PubMed:22327296"
FT   MUTAGEN         47
FT                   /note="K->A: Loss of phosphorylation; when associated with
FT                   A-46."
FT                   /evidence="ECO:0000269|PubMed:22327296"
FT   MUTAGEN         47
FT                   /note="K->E: Reduced interaction with MEN1; when associated
FT                   with E-46."
FT                   /evidence="ECO:0000269|PubMed:22327296"
FT   MUTAGEN         52
FT                   /note="L->A: Loss of phosphorylation; when associated with
FT                   A-54."
FT                   /evidence="ECO:0000269|PubMed:22327296"
FT   MUTAGEN         54
FT                   /note="L->A: Loss of phosphorylation; when associated with
FT                   A-52."
FT                   /evidence="ECO:0000269|PubMed:22327296"
FT   CONFLICT        24
FT                   /note="S -> T (in Ref. 1; CAA40010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        157
FT                   /note="A -> R (in Ref. 1; CAA40010)"
FT                   /evidence="ECO:0000305"
FT   HELIX           266..329
FT                   /evidence="ECO:0007829|PDB:5VPE"
SQ   SEQUENCE   347 AA;  35174 MW;  FE85A1AA2B5B9597 CRC64;
     METPFYGDEA LSGLGGGASG SGGSFASPGR LFPGAPPTAA AGSMMKKDAL TLSLSEQVAA
     ALKPAAAPPP TPLRADGAPS AAPPDGLLAS PDLGLLKLAS PELERLIIQS NGLVTTTPTS
     SQFLYPKVAA SEEQEFAEGF VKALEDLHKQ NQLGAGAAAA AAAAAAGGPS GTATGSAPPG
     ELAPAAAAPE APVYANLSSY AGGAGGAGGA ATVAFAAEPV PFPPPPPPGA LGPPRLAALK
     DEPQTVPDVP SFGESPPLSP IDMDTQERIK AERKRLRNRI AASKCRKRKL ERISRLEEKV
     KTLKSQNTEL ASTASLLREQ VAQLKQKVLS HVNSGCQLLP QHQVPAY
//
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