INS_PIG
ID INS_PIG Reviewed; 108 AA.
AC P01315; Q9TSJ5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Insulin;
DE Contains:
DE RecName: Full=Insulin B chain;
DE Contains:
DE RecName: Full=Insulin A chain;
DE Flags: Precursor;
GN Name=INS;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RA Han X.G., Tuch B.E.;
RT "Complete porcine preproinsulin cDNA sequence.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Large white;
RX PubMed=12140686; DOI=10.1007/s00335-001-3059-x;
RA Amarger V., Nguyen M., Van Laere A.-S., Braunschweig M., Nezer C.,
RA Georges M., Andersson L.;
RT "Comparative sequence analysis of the INS-IGF2-H19 gene cluster in pigs.";
RL Mamm. Genome 13:388-398(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=European wild boar, Hampshire, Japanese wild boar, Landrace,
RC Large white, Meishan, and Pietrain;
RX PubMed=14574411; DOI=10.1038/nature02064;
RA Van Laere A.-S., Nguyen M., Braunschweig M., Nezer C., Collette C.,
RA Moreau L., Archibald A.L., Haley C., Buys N., Tally M., Andersson G.,
RA Georges M., Andersson L.;
RT "A regulatory mutation in IGF2 causes a major QTL effect on muscle growth
RT in the pig.";
RL Nature 425:832-836(2003).
RN [4]
RP PROTEIN SEQUENCE OF 25-108.
RX PubMed=5657063; DOI=10.1126/science.161.3837.165;
RA Chance R.E., Ellis R.M., Bromer W.W.;
RT "Porcine proinsulin: characterization and amino acid sequence.";
RL Science 161:165-167(1968).
RN [5]
RP SEQUENCE REVISION TO 59.
RA Chance R.E.;
RL Submitted (JUL-1970) to the PIR data bank.
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RA Blundell T.L., Dodson G.G., Hodgkin D., Mercola D.;
RT "Insulin. The structure in the crystal and its reflection in chemistry and
RT biology.";
RL Adv. Protein Chem. 26:279-402(1972).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 88-108 AND 25-54, AND DISULFIDE
RP BONDS.
RA Isaacs N.W., Agarwal R.C.;
RT "Experience with fast Fourier least squares in the refinement of the
RT crystal structure of rhombohedral 2-zinc insulin at 1.5-A resolution.";
RL Acta Crystallogr. A 34:782-791(1978).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=2905485; DOI=10.1098/rstb.1988.0058;
RA Baker E.N., Blundell T.L., Cutfield J.F., Cutfield S.M., Dodson E.J.,
RA Dodson G.G., Crowfoot Hodgkin D.M., Hubbard R.E., Isaacs N.W.,
RA Reynolds C.D., Sakabe K., Sakabe N., Vijayan N.M.;
RT "The structure of 2Zn pig insulin crystals at 1.5-A resolution.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 319:369-456(1988).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 88-108 AND 25-54, AND DISULFIDE
RP BONDS.
RX PubMed=1772633; DOI=10.1107/s010876819100842x;
RA Balschmidt P., Hansen F.B., Dodson E., Dodson G., Korber F.;
RT "Structure of porcine insulin cocrystallized with clupeine Z.";
RL Acta Crystallogr. B 47:975-986(1991).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=2025410; DOI=10.1107/s0108768190009570;
RA Badger J., Harris M.R., Reynolds C.D., Evans A.C., Dodson E.J.,
RA Dodson G.G., North A.C.T.;
RT "Structure of the pig insulin dimer in the cubic crystal.";
RL Acta Crystallogr. B 47:127-136(1991).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 88-108 AND 27-49, AND DISULFIDE
RP BONDS.
RX PubMed=15299880; DOI=10.1107/s0907444997004034;
RA Diao J.-S., Wan Z.-L., Chang W.-R., Liang D.-C.;
RT "Structure of monomeric porcine DesB1-B2 despentapeptide (B26-B30) insulin
RT at 1.65-A resolution.";
RL Acta Crystallogr. D 53:507-512(1997).
CC -!- FUNCTION: Insulin decreases blood glucose concentration. It increases
CC cell permeability to monosaccharides, amino acids and fatty acids. It
CC accelerates glycolysis, the pentose phosphate cycle, and glycogen
CC synthesis in liver.
CC -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC disulfide bonds. {ECO:0000250|UniProtKB:P01308}.
CC -!- INTERACTION:
CC P01315; P01315: INS; NbExp=2; IntAct=EBI-8437944, EBI-8437944;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC77920.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Protein of the 20th century
CC - Issue 9 of April 2001;
CC URL="https://web.expasy.org/spotlight/back_issues/009";
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DR EMBL; AF064555; AAC77920.1; ALT_INIT; mRNA.
DR EMBL; AY044828; AAL69550.1; -; Genomic_DNA.
DR EMBL; AY242098; AAQ00952.1; -; Genomic_DNA.
DR EMBL; AY242099; AAQ00954.1; -; Genomic_DNA.
DR EMBL; AY242100; AAQ00957.1; -; Genomic_DNA.
DR EMBL; AY242101; AAQ00960.1; -; Genomic_DNA.
DR EMBL; AY242102; AAQ00963.1; -; Genomic_DNA.
DR EMBL; AY242103; AAQ00966.1; -; Genomic_DNA.
DR EMBL; AY242104; AAQ00969.1; -; Genomic_DNA.
DR EMBL; AY242105; AAQ00972.1; -; Genomic_DNA.
DR EMBL; AY242106; AAQ00975.1; -; Genomic_DNA.
DR EMBL; AY242107; AAQ00978.1; -; Genomic_DNA.
DR EMBL; AY242108; AAQ00981.1; -; Genomic_DNA.
DR EMBL; AY242109; AAQ00983.1; -; Genomic_DNA.
DR EMBL; AY242110; AAQ00985.1; -; Genomic_DNA.
DR EMBL; AY242111; AAQ00987.1; -; Genomic_DNA.
DR EMBL; AY242112; AAQ00990.1; -; Genomic_DNA.
DR PIR; A01583; IPPG.
DR RefSeq; NP_001103242.1; NM_001109772.1.
DR PDB; 1B17; X-ray; 1.70 A; A=88-108, B=25-54.
DR PDB; 1B18; X-ray; 1.80 A; A=88-108, B=25-54.
DR PDB; 1B19; X-ray; 1.80 A; A=88-108, B=25-54.
DR PDB; 1B2A; X-ray; 1.70 A; A=88-108, B=25-54.
DR PDB; 1B2B; X-ray; 1.80 A; A=88-108, B=25-54.
DR PDB; 1B2C; X-ray; 1.80 A; A=88-108, B=25-54.
DR PDB; 1B2D; X-ray; 1.70 A; A=88-108, B=25-54.
DR PDB; 1B2E; X-ray; 1.90 A; A=88-108, B=25-54.
DR PDB; 1B2F; X-ray; 1.90 A; A=88-108, B=25-54.
DR PDB; 1B2G; X-ray; 1.80 A; A=88-108, B=25-54.
DR PDB; 1DEI; X-ray; 1.60 A; A/C=88-108, B/D=25-47.
DR PDB; 1IZA; X-ray; 2.50 A; A/C=88-108, B/D=25-53.
DR PDB; 1IZB; X-ray; 2.00 A; A/C=88-108, B/D=25-53.
DR PDB; 1M5A; X-ray; 1.20 A; A/C=88-108, B/D=25-54.
DR PDB; 1MPJ; X-ray; 2.30 A; A/C=88-108, B/D=25-54.
DR PDB; 1SDB; X-ray; 1.65 A; A=88-108, B=27-49.
DR PDB; 1WAV; X-ray; 2.50 A; A/C/E/G/I/K=88-108, B/D/F/H/J/L=25-54.
DR PDB; 1ZEI; X-ray; 1.90 A; A/B/C/D/E/F=25-54, A/B/C/D/E/F=88-108.
DR PDB; 1ZNI; X-ray; 1.50 A; A/C=88-108, B/D=25-54.
DR PDB; 2EFA; Neutron; 2.70 A; A=88-108, B=25-54.
DR PDB; 2G4M; X-ray; 1.80 A; A=88-108, B=25-54.
DR PDB; 2TCI; X-ray; 1.80 A; A/C=88-108, B/D=25-54.
DR PDB; 2ZPP; Neutron; 2.50 A; A=88-108, B=25-54.
DR PDB; 3FHP; Neutron; 2.00 A; A/C=88-108, B/D=25-54.
DR PDB; 3GKY; X-ray; 1.80 A; A/C=88-108, B/D=25-54.
DR PDB; 3INS; X-ray; 1.50 A; A/C=88-108, B/D=25-54.
DR PDB; 3MTH; X-ray; 1.90 A; A/C=88-108, B/D=25-54.
DR PDB; 3RTO; X-ray; 1.80 A; A/C=88-108, B/D=25-54.
DR PDB; 3T2A; X-ray; 2.10 A; A=88-108, B=25-54.
DR PDB; 4A7E; X-ray; 1.86 A; A=88-108, B=25-54.
DR PDB; 4INS; X-ray; 1.50 A; A/C=88-108, B/D=25-54.
DR PDB; 5D52; X-ray; 1.80 A; A=88-108, B=25-54.
DR PDB; 5D53; X-ray; 1.50 A; A=88-108, B=25-54.
DR PDB; 5D54; X-ray; 1.50 A; A=88-108, B=25-54.
DR PDB; 5D5E; X-ray; 2.41 A; A=88-108, B=25-54.
DR PDB; 5FB6; X-ray; 1.90 A; A=88-108, B=25-54.
DR PDB; 5LIS; X-ray; 2.29 A; A=88-108, B=25-54.
DR PDB; 6INS; X-ray; 2.00 A; E/F=25-108.
DR PDB; 6Z7Z; X-ray; 2.40 A; E/G=88-108, F/H=25-54.
DR PDB; 7AC4; X-ray; 1.46 A; A=88-108, B=25-54.
DR PDB; 7INS; X-ray; 2.00 A; A/C/E=88-108, B/D/F=25-54.
DR PDB; 9INS; X-ray; 1.70 A; A=88-108, B=25-54.
DR PDBsum; 1B17; -.
DR PDBsum; 1B18; -.
DR PDBsum; 1B19; -.
DR PDBsum; 1B2A; -.
DR PDBsum; 1B2B; -.
DR PDBsum; 1B2C; -.
DR PDBsum; 1B2D; -.
DR PDBsum; 1B2E; -.
DR PDBsum; 1B2F; -.
DR PDBsum; 1B2G; -.
DR PDBsum; 1DEI; -.
DR PDBsum; 1IZA; -.
DR PDBsum; 1IZB; -.
DR PDBsum; 1M5A; -.
DR PDBsum; 1MPJ; -.
DR PDBsum; 1SDB; -.
DR PDBsum; 1WAV; -.
DR PDBsum; 1ZEI; -.
DR PDBsum; 1ZNI; -.
DR PDBsum; 2EFA; -.
DR PDBsum; 2G4M; -.
DR PDBsum; 2TCI; -.
DR PDBsum; 2ZPP; -.
DR PDBsum; 3FHP; -.
DR PDBsum; 3GKY; -.
DR PDBsum; 3INS; -.
DR PDBsum; 3MTH; -.
DR PDBsum; 3RTO; -.
DR PDBsum; 3T2A; -.
DR PDBsum; 4A7E; -.
DR PDBsum; 4INS; -.
DR PDBsum; 5D52; -.
DR PDBsum; 5D53; -.
DR PDBsum; 5D54; -.
DR PDBsum; 5D5E; -.
DR PDBsum; 5FB6; -.
DR PDBsum; 5LIS; -.
DR PDBsum; 6INS; -.
DR PDBsum; 6Z7Z; -.
DR PDBsum; 7AC4; -.
DR PDBsum; 7INS; -.
DR PDBsum; 9INS; -.
DR AlphaFoldDB; P01315; -.
DR BMRB; P01315; -.
DR SASBDB; P01315; -.
DR SMR; P01315; -.
DR IntAct; P01315; 1.
DR MINT; P01315; -.
DR STRING; 9823.ENSSSCP00000025428; -.
DR Allergome; 2122; Sus s Insulin.
DR PaxDb; P01315; -.
DR Ensembl; ENSSSCT00000064136; ENSSSCP00000044635; ENSSSCG00000033740.
DR Ensembl; ENSSSCT00015005290; ENSSSCP00015002060; ENSSSCG00015004005.
DR Ensembl; ENSSSCT00025032226; ENSSSCP00025013482; ENSSSCG00025023773.
DR Ensembl; ENSSSCT00030103634; ENSSSCP00030047908; ENSSSCG00030073948.
DR Ensembl; ENSSSCT00035025488; ENSSSCP00035009642; ENSSSCG00035019667.
DR Ensembl; ENSSSCT00040023180; ENSSSCP00040009750; ENSSSCG00040017207.
DR Ensembl; ENSSSCT00045008618; ENSSSCP00045005838; ENSSSCG00045005189.
DR Ensembl; ENSSSCT00050011348; ENSSSCP00050004834; ENSSSCG00050008342.
DR Ensembl; ENSSSCT00055032104; ENSSSCP00055025559; ENSSSCG00055016292.
DR Ensembl; ENSSSCT00060047539; ENSSSCP00060020355; ENSSSCG00060035069.
DR Ensembl; ENSSSCT00065087685; ENSSSCP00065038365; ENSSSCG00065063887.
DR Ensembl; ENSSSCT00070029958; ENSSSCP00070024989; ENSSSCG00070015252.
DR GeneID; 397415; -.
DR KEGG; ssc:397415; -.
DR CTD; 3630; -.
DR VGNC; VGNC:99778; INS.
DR eggNOG; ENOG502S5P5; Eukaryota.
DR GeneTree; ENSGT00390000015440; -.
DR InParanoid; P01315; -.
DR OMA; IVEQCCN; -.
DR OrthoDB; 1644517at2759; -.
DR EvolutionaryTrace; P01315; -.
DR Proteomes; UP000008227; Chromosome 2.
DR Proteomes; UP000314985; Unassembled WGS sequence.
DR Bgee; ENSSSCG00000033740; Expressed in right lobe of liver and 4 other tissues.
DR GO; GO:0005615; C:extracellular space; ISS:AgBase.
DR GO; GO:0005179; F:hormone activity; IMP:AgBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005158; F:insulin receptor binding; IEA:Ensembl.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; IMP:AgBase.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0032148; P:activation of protein kinase B activity; IEA:Ensembl.
DR GO; GO:0006953; P:acute-phase response; IEA:Ensembl.
DR GO; GO:0046631; P:alpha-beta T cell activation; IEA:Ensembl.
DR GO; GO:0055089; P:fatty acid homeostasis; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009101; P:glycoprotein biosynthetic process; IMP:AgBase.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0019249; P:lactate biosynthetic process; IMP:AgBase.
DR GO; GO:0008610; P:lipid biosynthetic process; IMP:AgBase.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IMP:AgBase.
DR GO; GO:0002674; P:negative regulation of acute inflammatory response; IEA:Ensembl.
DR GO; GO:0045922; P:negative regulation of fatty acid metabolic process; IEA:Ensembl.
DR GO; GO:2000252; P:negative regulation of feeding behavior; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IMP:AgBase.
DR GO; GO:0045818; P:negative regulation of glycogen catabolic process; IEA:Ensembl.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; IEA:Ensembl.
DR GO; GO:0033861; P:negative regulation of NAD(P)H oxidase activity; IEA:Ensembl.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0050709; P:negative regulation of protein secretion; IEA:Ensembl.
DR GO; GO:0045861; P:negative regulation of proteolysis; IEA:Ensembl.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IEA:Ensembl.
DR GO; GO:0060266; P:negative regulation of respiratory burst involved in inflammatory response; IEA:Ensembl.
DR GO; GO:1990535; P:neuron projection maintenance; IEA:Ensembl.
DR GO; GO:0038060; P:nitric oxide-cGMP-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0001819; P:positive regulation of cytokine production; IEA:Ensembl.
DR GO; GO:1902952; P:positive regulation of dendritic spine maintenance; IEA:Ensembl.
DR GO; GO:0045740; P:positive regulation of DNA replication; IDA:BHF-UCL.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IDA:CACAO.
DR GO; GO:0046326; P:positive regulation of glucose import; IEA:Ensembl.
DR GO; GO:0010907; P:positive regulation of glucose metabolic process; IDA:CACAO.
DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IEA:Ensembl.
DR GO; GO:0045821; P:positive regulation of glycolytic process; IEA:Ensembl.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IDA:CACAO.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IEA:Ensembl.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR GO; GO:0010750; P:positive regulation of nitric oxide mediated signal transduction; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; IDA:BHF-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0050714; P:positive regulation of protein secretion; IBA:GO_Central.
DR GO; GO:0060267; P:positive regulation of respiratory burst; IEA:Ensembl.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; IEA:Ensembl.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0022898; P:regulation of transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:1903576; P:response to L-arginine; ISS:AgBase.
DR GO; GO:0042311; P:vasodilation; IEA:Ensembl.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR CDD; cd04367; IlGF_insulin_like; 1.
DR InterPro; IPR004825; Insulin.
DR InterPro; IPR016179; Insulin-like.
DR InterPro; IPR036438; Insulin-like_sf.
DR InterPro; IPR022353; Insulin_CS.
DR InterPro; IPR022352; Insulin_family.
DR PANTHER; PTHR11454; PTHR11454; 1.
DR Pfam; PF00049; Insulin; 1.
DR PRINTS; PR00277; INSULIN.
DR PRINTS; PR00276; INSULINFAMLY.
DR SMART; SM00078; IlGF; 1.
DR SUPFAM; SSF56994; SSF56994; 1.
DR PROSITE; PS00262; INSULIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Glucose metabolism; Hormone;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:5657063"
FT PEPTIDE 25..54
FT /note="Insulin B chain"
FT /id="PRO_0000015879"
FT PROPEP 57..85
FT /note="C peptide"
FT /id="PRO_0000015880"
FT PEPTIDE 88..108
FT /note="Insulin A chain"
FT /id="PRO_0000015881"
FT DISULFID 31..94
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000269|PubMed:15299880,
FT ECO:0000269|PubMed:1772633, ECO:0000269|PubMed:2905485,
FT ECO:0007744|PDB:1SDB, ECO:0007744|PDB:4INS,
FT ECO:0007744|PDB:7INS"
FT DISULFID 43..107
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000269|PubMed:15299880,
FT ECO:0000269|PubMed:1772633, ECO:0000269|PubMed:2905485,
FT ECO:0007744|PDB:1SDB, ECO:0007744|PDB:4INS,
FT ECO:0007744|PDB:7INS"
FT DISULFID 93..98
FT /evidence="ECO:0000269|PubMed:15299880,
FT ECO:0000269|PubMed:1772633, ECO:0000269|PubMed:2905485,
FT ECO:0007744|PDB:1SDB, ECO:0007744|PDB:4INS,
FT ECO:0007744|PDB:7INS"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:1M5A"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:1M5A"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1M5A"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:1M5A"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:1M5A"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:1M5A"
SQ SEQUENCE 108 AA; 11672 MW; CB4491B429858EBE CRC64;
MALWTRLLPL LALLALWAPA PAQAFVNQHL CGSHLVEALY LVCGERGFFY TPKARREAEN
PQAGAVELGG GLGGLQALAL EGPPQKRGIV EQCCTSICSL YQLENYCN
