PEX3_HUMAN
ID PEX3_HUMAN Reviewed; 373 AA.
AC P56589; Q6FGP5;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Peroxisomal biogenesis factor 3;
DE AltName: Full=Peroxin-3;
DE AltName: Full=Peroxisomal assembly protein PEX3;
GN Name=PEX3;
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=9657383; DOI=10.1016/s0014-5793(98)00557-2;
RA Kammerer S., Holzinger A., Welsch U., Roscher A.A.;
RT "Cloning and characterization of the gene encoding the human peroxisomal
RT assembly protein Pex3p.";
RL FEBS Lett. 429:53-60(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10430017; DOI=10.1016/s0171-9335(99)80078-8;
RA Soukupova M., Sprenger C., Gorgas K., Kunau W.H., Dodt G.;
RT "Identification and characterization of the human peroxin PEX3.";
RL Eur. J. Cell Biol. 78:357-374(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10679269; DOI=10.1006/bbrc.2000.2193;
RA Muntau A.C., Holzinger A., Mayerhofer P.U., Gartner J., Roscher A.A.,
RA Kammerer S.;
RT "The human PEX3 gene encoding a peroxisomal assembly protein: genomic
RT organization, positional mapping, and mutation analysis in candidate
RT phenotypes.";
RL Biochem. Biophys. Res. Commun. 268:704-710(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND VARIANT
RP PBD10A GLU-138.
RC TISSUE=Liver;
RX PubMed=10848631; DOI=10.1091/mbc.11.6.2085;
RA Ghaedi K., Tamura S., Okumoto K., Matsuzono Y., Fujiki Y.;
RT "The peroxin pex3p initiates membrane assembly in peroxisome biogenesis.";
RL Mol. Biol. Cell 11:2085-2102(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kim J.W.;
RT "Identification of a human transforming gene.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin, and Uterus;
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 [10]
RP INTERACTION WITH PEX19.
RX PubMed=10704444; DOI=10.1083/jcb.148.5.931;
RA Sacksteder K.A., Jones J.M., South S.T., Li X., Liu Y., Gould S.J.;
RT "PEX19 binds multiple peroxisomal membrane proteins, is predominantly
RT cytoplasmic, and is required for peroxisome membrane synthesis.";
RL J. Cell Biol. 148:931-944(2000).
RN [11]
RP INTERACTION WITH PEX19, AND SUBCELLULAR LOCATION.
RX PubMed=11390669; DOI=10.1128/mcb.21.13.4413-4424.2001;
RA Fransen M., Wylin T., Brees C., Mannaerts G.P., Van Veldhoven P.P.;
RT "Human pex19p binds peroxisomal integral membrane proteins at regions
RT distinct from their sorting sequences.";
RL Mol. Cell. Biol. 21:4413-4424(2001).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF LEU-125 AND ASN-134.
RX PubMed=15007061; DOI=10.1083/jcb.200311131;
RA Fang Y., Morrell J.C., Jones J.M., Gould S.J.;
RT "PEX3 functions as a PEX19 docking factor in the import of class I
RT peroxisomal membrane proteins.";
RL J. Cell Biol. 164:863-875(2004).
RN [13]
RP INVOLVEMENT IN PBD-CG12 AND PBD10A.
RX PubMed=10958759; DOI=10.1086/303071;
RA Muntau A.C., Mayerhofer P.U., Paton B.C., Kammerer S., Roscher A.A.;
RT "Defective peroxisome membrane synthesis due to mutations in human PEX3
RT causes Zellweger syndrome, complementation group G.";
RL Am. J. Hum. Genet. 67:967-975(2000).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=21768384; DOI=10.1073/pnas.1103283108;
RA Yonekawa S., Furuno A., Baba T., Fujiki Y., Ogasawara Y., Yamamoto A.,
RA Tagaya M., Tani K.;
RT "Sec16B is involved in the endoplasmic reticulum export of the peroxisomal
RT membrane biogenesis factor peroxin 16 (Pex16) in mammalian cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12746-12751(2011).
RN [16]
RP INVOLVEMENT IN PBD10B, AND VARIANT PBD10B ARG-331.
RX PubMed=27557811; DOI=10.1007/8904_2016_10;
RA Maxit C., Denzler I., Marchione D., Agosta G., Koster J., Wanders R.J.,
RA Ferdinandusse S., Waterham H.R.;
RT "Novel PEX3 gene mutations resulting in a moderate Zellweger spectrum
RT disorder.";
RL JIMD Rep. 34:71-75(2017).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 49-373 IN COMPLEX WITH PEX19, AND
RP SUBUNIT.
RX PubMed=21102411; DOI=10.1038/emboj.2010.293;
RA Sato Y., Shibata H., Nakatsu T., Nakano H., Kashiwayama Y., Imanaka T.,
RA Kato H.;
RT "Structural basis for docking of peroxisomal membrane protein carrier
RT Pex19p onto its receptor Pex3p.";
RL EMBO J. 29:4083-4093(2010).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 41-373 IN COMPLEX WITH PEX19, AND
RP SUBUNIT.
RX PubMed=20554521; DOI=10.1074/jbc.m110.138503;
RA Schmidt F., Treiber N., Zocher G., Bjelic S., Steinmetz M.O., Kalbacher H.,
RA Stehle T., Dodt G.;
RT "Insights into peroxisome function from the structure of PEX3 in complex
RT with a soluble fragment of PEX19.";
RL J. Biol. Chem. 285:25410-25417(2010).
CC -!- FUNCTION: Involved in peroxisome biosynthesis and integrity. Assembles
CC membrane vesicles before the matrix proteins are translocated. As a
CC docking factor for PEX19, is necessary for the import of peroxisomal
CC membrane proteins in the peroxisomes. {ECO:0000269|PubMed:10848631,
CC ECO:0000269|PubMed:15007061}.
CC -!- SUBUNIT: Interacts with PEX19. {ECO:0000269|PubMed:10704444,
CC ECO:0000269|PubMed:11390669, ECO:0000269|PubMed:20554521,
CC ECO:0000269|PubMed:21102411}.
CC -!- INTERACTION:
CC P56589; Q9Y5Y5: PEX16; NbExp=4; IntAct=EBI-594885, EBI-981985;
CC P56589; P40855: PEX19; NbExp=47; IntAct=EBI-594885, EBI-594747;
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:10848631,
CC ECO:0000269|PubMed:11390669, ECO:0000269|PubMed:21768384}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:11390669}.
CC -!- TISSUE SPECIFICITY: Found in all examined tissues.
CC -!- DISEASE: Peroxisome biogenesis disorder complementation group 12 (PBD-
CC CG12) [MIM:614882]: A peroxisomal disorder arising from a failure of
CC protein import into the peroxisomal membrane or matrix. The peroxisome
CC biogenesis disorders (PBD group) are genetically heterogeneous with at
CC least 14 distinct genetic groups as concluded from complementation
CC studies. Include disorders are: Zellweger syndrome (ZWS), neonatal
CC adrenoleukodystrophy (NALD), infantile Refsum disease (IRD), and
CC classical rhizomelic chondrodysplasia punctata (RCDP). ZWS, NALD and
CC IRD are distinct from RCDP and constitute a clinical continuum of
CC overlapping phenotypes known as the Zellweger spectrum (PBD-ZSS).
CC {ECO:0000269|PubMed:10958759}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Peroxisome biogenesis disorder 10A (PBD10A) [MIM:614882]: A
CC fatal peroxisome biogenesis disorder belonging to the Zellweger disease
CC spectrum and clinically characterized by severe neurologic dysfunction
CC with profound psychomotor retardation, severe hypotonia and neonatal
CC seizures, craniofacial abnormalities, liver dysfunction, and
CC biochemically by the absence of peroxisomes. Additional features
CC include cardiovascular and skeletal defects, renal cysts, ocular
CC abnormalities, and hearing impairment. Most severely affected
CC individuals with the classic form of the disease (classic Zellweger
CC syndrome) die within the first year of life.
CC {ECO:0000269|PubMed:10848631, ECO:0000269|PubMed:10958759}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Peroxisome biogenesis disorder 10B (PBD10B) [MIM:617370]: A
CC moderately severe peroxisome biogenesis disorder belonging to the
CC Zellweger disease spectrum. PBD10B is characterized by neonatal
CC jaundice, dysmorphic features, delayed psychomotor development, axial
CC hypotonia that can progress to severe spastic paraparesis with
CC hyperreflexia, nephrocalcinosis, neurogenic bladder, nystagmus, and
CC cataracts. Laboratory studies show increased levels of very long-chain
CC fatty acids. Inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:27557811}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the peroxin-3 family. {ECO:0000305}.
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DR EMBL; AJ001625; CAA04879.1; -; mRNA.
DR EMBL; AJ131389; CAA10362.1; -; mRNA.
DR EMBL; AJ009866; CAA08904.1; -; Genomic_DNA.
DR EMBL; AJ009867; CAA08904.1; JOINED; Genomic_DNA.
DR EMBL; AJ009868; CAA08904.1; JOINED; Genomic_DNA.
DR EMBL; AJ009869; CAA08904.1; JOINED; Genomic_DNA.
DR EMBL; AJ009870; CAA08904.1; JOINED; Genomic_DNA.
DR EMBL; AJ009871; CAA08904.1; JOINED; Genomic_DNA.
DR EMBL; AJ009872; CAA08904.1; JOINED; Genomic_DNA.
DR EMBL; AJ009873; CAA08904.1; JOINED; Genomic_DNA.
DR EMBL; AJ009874; CAA08904.1; JOINED; Genomic_DNA.
DR EMBL; AB035307; BAA97993.1; -; mRNA.
DR EMBL; AY277600; AAQ18039.1; -; mRNA.
DR EMBL; CR542062; CAG46859.1; -; mRNA.
DR EMBL; AL031320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47866.1; -; Genomic_DNA.
DR EMBL; BC014551; AAH14551.1; -; mRNA.
DR EMBL; BC015506; AAH15506.1; -; mRNA.
DR CCDS; CCDS5199.1; -.
DR RefSeq; NP_003621.1; NM_003630.2.
DR PDB; 3AJB; X-ray; 2.50 A; A=49-373.
DR PDB; 3MK4; X-ray; 2.42 A; A=41-373.
DR PDBsum; 3AJB; -.
DR PDBsum; 3MK4; -.
DR AlphaFoldDB; P56589; -.
DR SMR; P56589; -.
DR BioGRID; 114076; 199.
DR ELM; P56589; -.
DR IntAct; P56589; 9.
DR MINT; P56589; -.
DR STRING; 9606.ENSP00000356563; -.
DR TCDB; 9.A.17.1.2; the integral membrane peroxisomal protein importer-2 (ppi2) family.
DR iPTMnet; P56589; -.
DR PhosphoSitePlus; P56589; -.
DR BioMuta; PEX3; -.
DR DMDM; 3914303; -.
DR EPD; P56589; -.
DR jPOST; P56589; -.
DR MassIVE; P56589; -.
DR PaxDb; P56589; -.
DR PeptideAtlas; P56589; -.
DR PRIDE; P56589; -.
DR ProteomicsDB; 56929; -.
DR Antibodypedia; 33142; 134 antibodies from 25 providers.
DR DNASU; 8504; -.
DR Ensembl; ENST00000367591.5; ENSP00000356563.4; ENSG00000034693.15.
DR GeneID; 8504; -.
DR KEGG; hsa:8504; -.
DR MANE-Select; ENST00000367591.5; ENSP00000356563.4; NM_003630.3; NP_003621.1.
DR UCSC; uc003qjl.4; human.
DR CTD; 8504; -.
DR DisGeNET; 8504; -.
DR GeneCards; PEX3; -.
DR GeneReviews; PEX3; -.
DR HGNC; HGNC:8858; PEX3.
DR HPA; ENSG00000034693; Low tissue specificity.
DR MalaCards; PEX3; -.
DR MIM; 603164; gene.
DR MIM; 614882; phenotype.
DR MIM; 617370; phenotype.
DR neXtProt; NX_P56589; -.
DR OpenTargets; ENSG00000034693; -.
DR Orphanet; 772; Infantile Refsum disease.
DR Orphanet; 44; Neonatal adrenoleukodystrophy.
DR Orphanet; 912; Zellweger syndrome.
DR PharmGKB; PA33200; -.
DR VEuPathDB; HostDB:ENSG00000034693; -.
DR eggNOG; KOG4444; Eukaryota.
DR GeneTree; ENSGT00390000008481; -.
DR HOGENOM; CLU_041367_2_0_1; -.
DR InParanoid; P56589; -.
DR OMA; WSLQMAI; -.
DR OrthoDB; 891261at2759; -.
DR PhylomeDB; P56589; -.
DR TreeFam; TF352826; -.
DR PathwayCommons; P56589; -.
DR Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-HSA-9603798; Class I peroxisomal membrane protein import.
DR SignaLink; P56589; -.
DR SIGNOR; P56589; -.
DR BioGRID-ORCS; 8504; 39 hits in 1085 CRISPR screens.
DR EvolutionaryTrace; P56589; -.
DR GeneWiki; PEX3; -.
DR GenomeRNAi; 8504; -.
DR Pharos; P56589; Tbio.
DR PRO; PR:P56589; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P56589; protein.
DR Bgee; ENSG00000034693; Expressed in adrenal tissue and 206 other tissues.
DR ExpressionAtlas; P56589; baseline and differential.
DR Genevisible; P56589; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005778; C:peroxisomal membrane; HDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0032994; C:protein-lipid complex; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0007031; P:peroxisome organization; IMP:UniProtKB.
DR GO; GO:0045046; P:protein import into peroxisome membrane; IMP:UniProtKB.
DR InterPro; IPR006966; Peroxin-3.
DR PANTHER; PTHR28080; PTHR28080; 1.
DR Pfam; PF04882; Peroxin-3; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; Membrane; Peroxisome; Peroxisome biogenesis;
KW Peroxisome biogenesis disorder; Reference proteome; Transmembrane;
KW Transmembrane helix; Zellweger syndrome.
FT CHAIN 1..373
FT /note="Peroxisomal biogenesis factor 3"
FT /id="PRO_0000208737"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..116
FT /note="Peroxisomal"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..45
FT /note="Targeting to peroxisomes"
FT /evidence="ECO:0000269|PubMed:11390669"
FT REGION 120..136
FT /note="Interaction with PEX19"
FT /evidence="ECO:0000269|PubMed:11390669"
FT VARIANT 82
FT /note="Q -> R (in dbSNP:rs35220041)"
FT /id="VAR_053572"
FT VARIANT 138
FT /note="G -> E (in PBD10A)"
FT /evidence="ECO:0000269|PubMed:10848631"
FT /id="VAR_009304"
FT VARIANT 331
FT /note="G -> R (in PBD10B; dbSNP:rs1057523689)"
FT /evidence="ECO:0000269|PubMed:27557811"
FT /id="VAR_078657"
FT MUTAGEN 125
FT /note="L->P: Abolishes binding to PEX19 without affecting
FT targeting to peroxisomes; when associated with D-134."
FT /evidence="ECO:0000269|PubMed:15007061"
FT MUTAGEN 134
FT /note="N->D: Abolishes binding to PEX19 without affecting
FT targeting to peroxisomes; when associated with P-125."
FT /evidence="ECO:0000269|PubMed:15007061"
FT HELIX 41..83
FT /evidence="ECO:0007829|PDB:3MK4"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:3MK4"
FT HELIX 100..142
FT /evidence="ECO:0007829|PDB:3MK4"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:3AJB"
FT HELIX 158..165
FT /evidence="ECO:0007829|PDB:3MK4"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:3MK4"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:3MK4"
FT HELIX 174..191
FT /evidence="ECO:0007829|PDB:3MK4"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:3MK4"
FT HELIX 202..217
FT /evidence="ECO:0007829|PDB:3MK4"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:3MK4"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:3AJB"
FT HELIX 255..271
FT /evidence="ECO:0007829|PDB:3MK4"
FT HELIX 274..296
FT /evidence="ECO:0007829|PDB:3MK4"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:3MK4"
FT HELIX 322..330
FT /evidence="ECO:0007829|PDB:3MK4"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:3MK4"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:3AJB"
FT HELIX 344..349
FT /evidence="ECO:0007829|PDB:3MK4"
FT HELIX 352..366
FT /evidence="ECO:0007829|PDB:3MK4"
SQ SEQUENCE 373 AA; 42140 MW; 3515A1F29656B7CC CRC64;
MLRSVWNFLK RHKKKCIFLG TVLGGVYILG KYGQKKIREI QEREAAEYIA QARRQYHFES
NQRTCNMTVL SMLPTLREAL MQQLNSESLT ALLKNRPSNK LEIWEDLKII SFTRSTVAVY
STCMLVVLLR VQLNIIGGYI YLDNAAVGKN GTTILAPPDV QQQYLSSIQH LLGDGLTELI
TVIKQAVQKV LGSVSLKHSL SLLDLEQKLK EIRNLVEQHK SSSWINKDGS KPLLCHYMMP
DEETPLAVQA CGLSPRDITT IKLLNETRDM LESPDFSTVL NTCLNRGFSR LLDNMAEFFR
PTEQDLQHGN SMNSLSSVSL PLAKIIPIVN GQIHSVCSET PSHFVQDLLT MEQVKDFAAN
VYEAFSTPQQ LEK
