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UniProtKB/Swiss-Prot entry P21796


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name VDAC1_HUMAN
Primary accession number P21796
Secondary accession numbers Q5FVE7 Q9UIQ5 Q9UPL0
Integrated into Swiss-Prot on May 1, 1991
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 104)
Name and origin of the protein
Protein name Voltage-dependent anion-selective channel protein 1
Synonyms VDAC-1
hVDAC1
Outer mitochondrial membrane protein porin 1
Plasmalemmal porin
Porin 31HL
Porin 31HM
Gene name
Name: VDAC1
Synonyms: VDAC
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8420959 [NCBI, ExPASy, EBI, Israel, Japan]
Blachly-Dyson E., Zambronicz E.B., Yu W.H., Adams V., McCabe E.R., Adelman J.P., Colombini M., Forte M.A.;
"Cloning and functional expression in yeast of two human isoforms of the outer mitochondrial membrane channel, the voltage-dependent anion channel.";
J. Biol. Chem. 268:1835-1841(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pituitary;
Blachly-Dyson E., Forte M.A.;
"Cloning of human VDAC cDNA.";
Biophys. J. 59:216A-216A(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1007/s003359901158; PubMed=10501981 [NCBI, ExPASy, EBI, Israel, Japan]
Decker W.K., Bowles K.R., Schatte E.C., Towbin J.A., Craigen W.J.;
"Revised fine mapping of the human voltage-dependent anion channel loci by radiation hybrid analysis.";
Mamm. Genome 10:1041-1042(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1006/bbrc.2000.2487; PubMed=10772903 [NCBI, ExPASy, EBI, Israel, Japan]
Messina A., Guarino F., Oliva M., van den Heuvel L.P., Smeitink J., De Pinto V.;
"Characterization of the human porin isoform 1 (HVDAC1) gene by amplification on the whole human genome: a tool for porin deficiency analysis.";
Biochem. Biophys. Res. Commun. 270:787-792(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02919; PubMed=15372022 [NCBI, ExPASy, EBI, Israel, Japan]
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
PROTEIN SEQUENCE OF 2-283.
TISSUE=Lymphocyte;
PubMed=2559745 [NCBI, ExPASy, EBI, Israel, Japan]
Kayser H., Kratzin H.D., Thinnes F.P., Goetz H., Schmidt W.E., Eckart K., Hilschmann N.;
"Identification of human porins. II. Characterization and primary structure of a 31-lDa porin from human B lymphocytes (Porin 31HL).";
Biol. Chem. Hoppe-Seyler 370:1265-1278(1989).
[8]
PROTEIN SEQUENCE OF 2-283.
TISSUE=Skeletal muscle;
PubMed=1657034 [NCBI, ExPASy, EBI, Israel, Japan]
Juergens L., Ilsemann P., Kratzin H.D., Hesse D., Eckart K., Thinnes F.P., Hilschmann N.;
"Studies on human porin. IV. The primary structures of 'Porin 31HM' purified from human skeletal muscle membranes and of 'Porin 31HL' derived from human B lymphocyte membranes are identical.";
Biol. Chem. Hoppe-Seyler 372:455-463(1991).
[9]
PROTEIN SEQUENCE OF 2-283.
TISSUE=B-cell;
Hein A., Kiafard Z., Hesse D., Hesse J.-O., Zimmermann B., Kratzin H.D., Schulz H., Reiss J., Thinnes F.P., Goetz H., Hilschmann N.;
Submitted (DEC-1997) to UniProtKB.
[10]
PROTEIN SEQUENCE OF 2-12; 21-61; 64-74; 94-110; 121-139; 162-174; 225-236 AND 257-274, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (MAR-2005) to UniProtKB.
[11]
PROTEIN SEQUENCE OF 175-197, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[12]
MUTAGENESIS.
PubMed=7685903 [NCBI, ExPASy, EBI, Israel, Japan]
Thomas L., Blachly-Dyson E., Colombini M., Forte M.A.;
"Mapping of residues forming the voltage sensor of the voltage-dependent anion-selective channel.";
Proc. Natl. Acad. Sci. U.S.A. 90:5446-5449(1993).
[13]
SUBCELLULAR LOCATION.
DOI=10.1074/jbc.270.23.13998; PubMed=7539795 [NCBI, ExPASy, EBI, Israel, Japan]
Yu W.H., Wolfgang W., Forte M.A.;
"Subcellular localization of human voltage-dependent anion channel isoforms.";
J. Biol. Chem. 270:13998-14006(1995).
[14]
CHARACTERIZATION, AND PARTIAL PROTEIN SEQUENCE.
DOI=10.1515/BC.1999.189; PubMed=10661876 [NCBI, ExPASy, EBI, Israel, Japan]
Stadtmueller U., Eben-Brunnen J., Schmid A., Hesse D., Klebert S., Kratzin H.D., Hesse J., Zimmermann B., Reymann S., Thinnes F.P., Benz R., Goetz H., Hilschmann N.;
"Mitochondria-derived and extra-mitochondrial human type-1 porin are identical as revealed by amino acid sequencing and electrophysiological characterisation.";
Biol. Chem. 380:1461-1466(1999).
[15]
FUNCTION.
DOI=10.1007/s004240100656; PubMed=11845315 [NCBI, ExPASy, EBI, Israel, Japan]
Thinnes F.P., Walter G., Hellmann K.P., Hellmann T., Merker R., Kiafard Z., Eben-Brunnen J., Schwarzer C., Goetz H., Hilschmann N.;
"Gadolinium as an opener of the outwardly rectifying Cl(-) channel (ORCC). Is there relevance for cystic fibrosis therapy?";
Pflugers Arch. 443:S111-S116(2001).
[16]
FUNCTION IN APOPTOSIS.
DOI=10.1196/annals.1299.022; PubMed=15033708 [NCBI, ExPASy, EBI, Israel, Japan]
Verrier F., Mignotte B., Jan G., Brenner C.;
"Study of PTPC composition during apoptosis for identification of viral protein target.";
Ann. N. Y. Acad. Sci. 1010:126-142(2003).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-195, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[19]
INTERACTION WITH INFLUENZA A VIRUS PB1-F2.
DOI=10.1371/journal.ppat.0010004; PubMed=16201016 [NCBI, ExPASy, EBI, Israel, Japan]
Zamarin D., Garcia-Sastre A., Xiao X., Wang R., Palese P.;
"Influenza virus PB1-F2 protein induces cell death through mitochondrial ANT3 and VDAC1.";
PLoS Pathog. 1:40-54(2005).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0507066103; PubMed=16565220 [NCBI, ExPASy, EBI, Israel, Japan]
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
"Phosphoproteome analysis of the human mitotic spindle.";
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[24]
X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) OF 2-283, AND STRUCTURE BY NMR.
DOI=10.1073/pnas.0808115105; PubMed=18832158 [NCBI, ExPASy, EBI, Israel, Japan]
Bayrhuber M., Meins T., Habeck M., Becker S., Giller K., Villinger S., Vonrhein C., Griesinger C., Zweckstetter M., Zeth K.;
"Structure of the human voltage-dependent anion channel.";
Proc. Natl. Acad. Sci. U.S.A. 105:15370-15375(2008).
[25]
STRUCTURE BY NMR, FUNCTION, INTERACTION WITH BCL2L1, AND NADH BINDING.
DOI=10.1126/science.1161302; PubMed=18755977 [NCBI, ExPASy, EBI, Israel, Japan]
Hiller S., Garces R.G., Malia T.J., Orekhov V.Y., Colombini M., Wagner G.;
"Solution structure of the integral human membrane protein VDAC-1 in detergent micelles.";
Science 321:1206-1210(2008).
Comments
  • FUNCTION: Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis.
  • SUBUNIT: Interacts with hexokinases (By similarity). Interacts with BCL2L1. Interacts with influenza A virus PB1-F2 protein.
  • INTERACTION:
    P81605:DCD; NbExp=1; IntAct=EBI-354158, EBI-395625;
    P60520:GABARAPL2; NbExp=1; IntAct=EBI-354158, EBI-720116;
    P33176:KIF5B; NbExp=1; IntAct=EBI-354158, EBI-355878;
    P23508:MCC; NbExp=1; IntAct=EBI-354158, EBI-307531;
    Q9Y4K3:TRAF6; NbExp=1; IntAct=EBI-354158, EBI-359276;
  • SUBCELLULAR LOCATION: Mitochondrion outer membrane. Cell membrane.
  • TISSUE SPECIFICITY: Heart, liver and skeletal muscle.
  • DOMAIN: Consists mainly of a membrane-spanning beta-barrel formed by 19 beta-strands. The helical N-terminus folds back into the pore opening and plays a role in voltage-gated channel activity.
  • SIMILARITY: Belongs to the eukaryotic mitochondrial porin family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L06132; AAA61272.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ250032; CAB58127.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ250033; CAB58127.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ250034; CAB58127.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ250035; CAB58127.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ250036; CAB58127.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ250037; CAB58127.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ250038; CAB58127.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ250039; CAB58127.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF151097; AAD54939.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF151093; AAD54939.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF151094; AAD54939.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF151095; AAD54939.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF151096; AAD54939.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC005200; AAC24723.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC008608; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
BC008482; AAH08482.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC071168; AAH71168.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC090042; AAH90042.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A44422; MMHUP3.
RefSeq NP_003365.1; -.
UniGene Hs.519320
3D structure databases
PDB
2JK4; X-ray; 4.10 A; A=2-283.[ExPASy / RCSB / EBI]
2K4T; NMR; -; A=1-283.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
ModBase P21796.
Protein-protein interaction databases
IntAct P21796; -.
PTM databases
PhosphoSite P21796; -.
2D gel databases
DOSAC-COBS-2DPAGE P21796; -.
OGP P21796; -.
REPRODUCTION-2DPAGE IPI00216308; -.
P21796; -.
Organism-specific databases
H-InvDB HIX0005171; -.
HGNC HGNC:12669; VDAC1.
GenAtlas VDAC1.
HPA CAB005885; -.
MIM 604492; gene+phenotype. [NCBI / EBI]
PharmGKB PA37292; -.
GeneCards P21796.
Gene expression databases
ArrayExpress P21796; -.
CleanEx HS_VDAC1; -.
GermOnline ENSG00000073905; Homo sapiens.
Ontologies
GO
GO:0005741; Cellular component: mitochondrial outer membrane (traceable author statement from ProtInc).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0046930; Cellular component: pore complex (traceable author statement from HGNC).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0008308; Molecular function: voltage-gated anion channel activity (traceable author statement from UniProtKB).
GO:0006820; Biological process: anion transport (traceable author statement from ProtInc).
GO:0008632; Biological process: apoptotic program (traceable author statement from ProtInc).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001925; Porin_Euk.
Graphical view of domain structure.
Pfam PF01459; Porin_3; 1.
Pfam graphical view of domain structure.
PRINTS PR00185; EUKARYTPORIN.
PROSITE PS00558; EUKARYOTIC_PORIN; 1.
ProtoNet P21796.
Proteomic databases
PeptideAtlas P21796; -.
Genome annotation databases
Ensembl ENSG00000213585; Homo sapiens. [Contig view]
GeneID 7416; -.
KEGG hsa:7416; -.
Phylogenomic databases
HOGENOM P21796; -.
HOVERGEN P21796; -.
Other
DrugBank DB01375; Dihydroxyaluminium.
LinkHub P21796; -.
NextBio 29038; -.
SOURCE VDAC1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Apoptosis; Cell membrane; Direct protein sequencing; Host-virus interaction; Ion transport; Membrane; Mitochondrion; Mitochondrion outer membrane; Phosphoprotein; Porin; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   283  282     Voltage-dependent anion-selective channel protein 1. PRO_0000050499
TRANSMEM   26    35  10     Transmembrane beta-strand. 
TRANSMEM   39    47  9     Transmembrane beta-strand. 
TRANSMEM   54    64  11     Transmembrane beta-strand. 
TRANSMEM   69    76  8     Transmembrane beta-strand. 
TRANSMEM   80    89  10     Transmembrane beta-strand. 
TRANSMEM   95   104  10     Transmembrane beta-strand. 
TRANSMEM   111   120  10     Transmembrane beta-strand. 
TRANSMEM   123   130  8     Transmembrane beta-strand. 
TRANSMEM   137   145  9     Transmembrane beta-strand. 
TRANSMEM   150   158  9     Transmembrane beta-strand. 
TRANSMEM   163   175  13     Transmembrane beta-strand. 
TRANSMEM   178   185  8     Transmembrane beta-strand. 
TRANSMEM   189   198  10     Transmembrane beta-strand. 
TRANSMEM   202   211  10     Transmembrane beta-strand. 
TRANSMEM   218   227  10     Transmembrane beta-strand. 
TRANSMEM   231   238  8     Transmembrane beta-strand. 
TRANSMEM   242   251  10     Transmembrane beta-strand. 
TRANSMEM   254   263  10     Transmembrane beta-strand. 
TRANSMEM   273   282  10     Transmembrane beta-strand. 
NP_BIND   242   244  3     NAD. 
NP_BIND   260   264  5     NAD. 
SITE   73    73  1     Involved in hexokinase binding (By similarity). 
MOD_RES   2     2        N-acetylalanine. 
MOD_RES   13    13        Phosphoserine (By similarity). 
MOD_RES   20    20        N6-acetyllysine (By similarity). 
MOD_RES   28    28        N6-acetyllysine (By similarity). 
MOD_RES   61    61        N6-acetyllysine (By similarity). 
MOD_RES   67    67        Phosphotyrosine. 
MOD_RES   104   104        Phosphoserine. 
MOD_RES   137   137        Phosphoserine (By similarity). 
MOD_RES   195   195        Phosphotyrosine. 
MOD_RES   224   224        N6-acetyllysine (By similarity). 
CONFLICT   225   225        Y -> L (in Ref. 4; CAB58127). 
Sequence information
Length: 283 AA [This is the length of the unprocessed precursor] Molecular weight: 30773 Da [This is the MW of the unprocessed precursor] CRC64: 89BA3378B04020D5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAVPPTYADL GKSARDVFTK GYGFGLIKLD LKTKSENGLE FTSSGSANTE TTKVTGSLET 

        70         80         90        100        110        120 
KYRWTEYGLT FTEKWNTDNT LGTEITVEDQ LARGLKLTFD SSFSPNTGKK NAKIKTGYKR 

       130        140        150        160        170        180 
EHINLGCDMD FDIAGPSIRG ALVLGYEGWL AGYQMNFETA KSRVTQSNFA VGYKTDEFQL 

       190        200        210        220        230        240 
HTNVNDGTEF GGSIYQKVNK KLETAVNLAW TAGNSNTRFG IAAKYQIDPD ACFSAKVNNS 

       250        260        270        280 
SLIGLGYTQT LKPGIKLTLS ALLDGKNVNA GGHKLGLGLE FQA 

P21796 in FASTA format

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