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-MAY-2023, entry version 186. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 200. 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 GlyGen; P56589; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P56589; -. DR PhosphoSitePlus; P56589; -. DR SwissPalm; P56589; -. DR BioMuta; PEX3; -. DR DMDM; 3914303; -. DR EPD; P56589; -. DR jPOST; P56589; -. DR MassIVE; P56589; -. DR PaxDb; P56589; -. DR PeptideAtlas; 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 AGR; HGNC:8858; -. 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; HRGWKDL; -. DR OrthoDB; 5477008at2759; -. 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; 41 hits in 1162 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:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB. DR GO; GO:0005777; C:peroxisome; IDA:MGI. 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; PEROXISOMAL BIOGENESIS FACTOR 3; 1. DR PANTHER; PTHR28080:SF1; PEROXISOMAL BIOGENESIS FACTOR 3; 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 //