GAN_HUMAN
ID GAN_HUMAN Reviewed; 597 AA.
AC Q9H2C0;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Gigaxonin;
DE AltName: Full=Kelch-like protein 16;
GN Name=GAN; Synonyms=GAN1, KLHL16;
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], AND VARIANTS GAN1 SER-15; GLY-52; LEU-79;
RP PHE-82; HIS-138; GLN-269; ARG-309; LYS-486; CYS-545 AND TYR-570.
RC TISSUE=Brain;
RX PubMed=11062483; DOI=10.1038/81701;
RA Bomont P., Cavalier L., Blondeau F., Ben-Hamida C., Belal S., Tazir M.,
RA Demir E., Topaloglu H., Korinthenberg R., Tueysuez B., Landrieu P.,
RA Hentati F., Koenig M.;
RT "The gene encoding gigaxonin, a new member of the cytoskeletal BTB/kelch
RT repeat family, is mutated in giant axonal neuropathy.";
RL Nat. Genet. 26:370-374(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [3]
RP FUNCTION, INTERACTION WITH MAP1B, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12147674; DOI=10.1083/jcb.200202055;
RA Ding J., Liu J.-J., Kowal A.S., Nardine T., Bhattacharya P., Lee A.,
RA Yang Y.;
RT "Microtubule-associated protein 1B: a neuronal binding partner for
RT gigaxonin.";
RL J. Cell Biol. 158:427-433(2002).
RN [4]
RP INTERACTION WITH CUL3.
RX PubMed=14528312; DOI=10.1038/ncb1056;
RA Furukawa M., He Y.J., Borchers C., Xiong Y.;
RT "Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin
RT ligases.";
RL Nat. Cell Biol. 5:1001-1007(2003).
RN [5]
RP FUNCTION, INTERACTION WITH TBCB, AND CHARACTERIZATION OF VARIANTS GAN1
RP SER-15; PHE-82 AND CYS-545.
RX PubMed=16303566; DOI=10.1016/j.cub.2005.10.052;
RA Wang W., Ding J., Allen E., Zhu P., Zhang L., Vogel H., Yang Y.;
RT "Gigaxonin interacts with tubulin folding cofactor B and controls its
RT degradation through the ubiquitin-proteasome pathway.";
RL Curr. Biol. 15:2050-2055(2005).
RN [6]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH CUL3 AND RBX1, AND
RP UBIQUITINATION.
RX PubMed=15983046; DOI=10.1074/jbc.m501279200;
RA Zhang D.D., Lo S.C., Sun Z., Habib G.M., Lieberman M.W., Hannink M.;
RT "Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3,
RT targets Keap1 for degradation by a proteasome-independent pathway.";
RL J. Biol. Chem. 280:30091-30099(2005).
RN [7]
RP FUNCTION, AND INTERACTION WITH UBA1 AND MAP1B.
RX PubMed=16227972; DOI=10.1038/nature04256;
RA Allen E., Ding J., Wang W., Pramanik S., Chou J., Yau V., Yang Y.;
RT "Gigaxonin-controlled degradation of MAP1B light chain is critical to
RT neuronal survival.";
RL Nature 438:224-228(2005).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=19424503; DOI=10.1371/journal.pone.0005492;
RA Wang X.J., Zhang D.D.;
RT "Ectodermal-neural cortex 1 down-regulates Nrf2 at the translational
RT level.";
RL PLoS ONE 4:E5492-E5492(2009).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-254.
RX PubMed=19818708; DOI=10.1016/j.molcel.2009.09.022;
RA Zhuang M., Calabrese M.F., Liu J., Waddell M.B., Nourse A., Hammel M.,
RA Miller D.J., Walden H., Duda D.M., Seyedin S.N., Hoggard T., Harper J.W.,
RA White K.P., Schulman B.A.;
RT "Structures of SPOP-substrate complexes: insights into molecular
RT architectures of BTB-Cul3 ubiquitin ligases.";
RL Mol. Cell 36:39-50(2009).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 6-126.
RG Structural genomics consortium (SGC);
RT "Structure of the BTB (tramtrack and bric a brac) domain of human
RT gigaxonin.";
RL Submitted (JUL-2011) to the PDB data bank.
RN [11]
RP VARIANT GAN1 THR-423.
RX PubMed=11971098; DOI=10.1212/wnl.58.8.1273;
RA Kuhlenbaumer G., Young P., Oberwittler C., Hunermund G., Schirmacher A.,
RA Domschke K., Ringelstein B., Stogbauer F.;
RT "Giant axonal neuropathy (GAN): case report and two novel mutations in the
RT gigaxonin gene.";
RL Neurology 58:1273-1276(2002).
RN [12]
RP ERRATUM OF PUBMED:11971098.
RA Kuhlenbaumer G., Young P., Oberwittler C., Hunermund G., Schirmacher A.,
RA Domschke K., Ringelstein B., Stogbauer F.;
RL Neurology 58:1444-1444(2002).
RN [13]
RP VARIANTS GAN1 PHE-86; GLN-269 AND ARG-368.
RX PubMed=12655563; DOI=10.1002/humu.9122;
RA Bomont P., Ioos C., Yalcinkaya C., Korinthenberg R., Vallat J.-M.,
RA Assami S., Munnich A., Chabrol B., Kurlemann G., Tazir M., Koenig M.;
RT "Identification of seven novel mutations in the GAN gene.";
RL Hum. Mutat. 21:446-446(2003).
RN [14]
RP VARIANTS GAN1 PRO-51 AND LEU-315.
RX PubMed=17578852; DOI=10.1136/jnnp.2007.118968;
RA Houlden H., Groves M., Miedzybrodzka Z., Roper H., Willis T., Winer J.,
RA Cole G., Reilly M.M.;
RT "New mutations, genotype phenotype studies and manifesting carriers in
RT giant axonal neuropathy.";
RL J. Neurol. Neurosurg. Psych. 78:1267-1270(2007).
RN [15]
RP VARIANTS GAN1 CYS-89; PHE-195; ARG-368; THR-423; ARG-474 AND HIS-545.
RX PubMed=17587580; DOI=10.1016/j.nmd.2007.03.012;
RA Koop O., Schirmacher A., Nelis E., Timmerman V., De Jonghe P.,
RA Ringelstein B., Rasic V.M., Evrard P., Gaertner J., Claeys K.G.,
RA Appenzeller S., Rautenstrauss B., Huehne K., Ramos-Arroyo M.A., Woerle H.,
RA Moilanen J.S., Hammans S., Kuhlenbaeumer G.;
RT "Genotype-phenotype analysis in patients with giant axonal neuropathy
RT (GAN).";
RL Neuromuscul. Disord. 17:624-630(2007).
RN [16]
RP VARIANTS THR-102 AND ILE-438.
RX PubMed=24627108; DOI=10.1007/s00415-014-7289-8;
RA Schabhuettl M., Wieland T., Senderek J., Baets J., Timmerman V.,
RA De Jonghe P., Reilly M.M., Stieglbauer K., Laich E., Windhager R., Erwa W.,
RA Trajanoski S., Strom T.M., Auer-Grumbach M.;
RT "Whole-exome sequencing in patients with inherited neuropathies: outcome
RT and challenges.";
RL J. Neurol. 261:970-982(2014).
CC -!- FUNCTION: Probable cytoskeletal component that directly or indirectly
CC plays an important role in neurofilament architecture. May act as a
CC substrate-specific adapter of an E3 ubiquitin-protein ligase complex
CC which mediates the ubiquitination and subsequent proteasomal
CC degradation of target proteins. Controls degradation of TBCB. Controls
CC degradation of MAP1B and MAP1S, and is critical for neuronal
CC maintenance and survival. {ECO:0000269|PubMed:12147674,
CC ECO:0000269|PubMed:15983046, ECO:0000269|PubMed:16227972,
CC ECO:0000269|PubMed:16303566}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with TBCB. Interacts with CUL3. Part of a complex
CC that contains CUL3, RBX1 and GAN. Interacts (via BTB domain) with UBA1.
CC Interacts (via Kelch domains) with MAP1B (via C-terminus) and MAP1S
CC (via C-terminus). {ECO:0000269|PubMed:12147674,
CC ECO:0000269|PubMed:14528312, ECO:0000269|PubMed:15983046,
CC ECO:0000269|PubMed:16227972, ECO:0000269|PubMed:16303566}.
CC -!- INTERACTION:
CC Q9H2C0; P46821: MAP1B; NbExp=3; IntAct=EBI-764342, EBI-764611;
CC Q9H2C0; Q8IVD9: NUDCD3; NbExp=2; IntAct=EBI-764342, EBI-744342;
CC Q9H2C0; O60260-5: PRKN; NbExp=3; IntAct=EBI-764342, EBI-21251460;
CC Q9H2C0; Q99426: TBCB; NbExp=3; IntAct=EBI-764342, EBI-764356;
CC Q9H2C0; P22314: UBA1; NbExp=5; IntAct=EBI-764342, EBI-709688;
CC Q9H2C0; P40337-2: VHL; NbExp=3; IntAct=EBI-764342, EBI-12157263;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart and muscle.
CC {ECO:0000269|PubMed:12147674}.
CC -!- PTM: Ubiquitinated by E3 ubiquitin ligase complex formed by CUL3 and
CC RBX1 and probably targeted for proteasome-independent degradation.
CC {ECO:0000269|PubMed:15983046}.
CC -!- DISEASE: Giant axonal neuropathy 1, autosomal recessive (GAN1)
CC [MIM:256850]: A severe autosomal recessive sensorimotor neuropathy
CC affecting both the peripheral nerves and the central nervous system.
CC Axonal loss and the presence of giant axonal swellings filled with
CC neurofilaments on nerve biopsies are the hallmarks of this
CC neurodegenerative disorder. {ECO:0000269|PubMed:11062483,
CC ECO:0000269|PubMed:11971098, ECO:0000269|PubMed:12655563,
CC ECO:0000269|PubMed:16303566, ECO:0000269|PubMed:17578852,
CC ECO:0000269|PubMed:17587580}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=Inherited peripheral neuropathies mutation db;
CC URL="https://uantwerpen.vib.be/CMTMutations";
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DR EMBL; AF291673; AAG35311.1; -; mRNA.
DR EMBL; BC044840; AAH44840.1; -; mRNA.
DR CCDS; CCDS10935.1; -.
DR RefSeq; NP_071324.1; NM_022041.3.
DR PDB; 2PPI; X-ray; 2.40 A; A=6-126.
DR PDB; 3HVE; X-ray; 2.80 A; A/B=1-254.
DR PDBsum; 2PPI; -.
DR PDBsum; 3HVE; -.
DR AlphaFoldDB; Q9H2C0; -.
DR SMR; Q9H2C0; -.
DR BioGRID; 113800; 260.
DR CORUM; Q9H2C0; -.
DR IntAct; Q9H2C0; 28.
DR MINT; Q9H2C0; -.
DR STRING; 9606.ENSP00000476795; -.
DR GlyGen; Q9H2C0; 9 sites, 1 O-linked glycan (9 sites).
DR iPTMnet; Q9H2C0; -.
DR PhosphoSitePlus; Q9H2C0; -.
DR BioMuta; GAN; -.
DR DMDM; 13626745; -.
DR EPD; Q9H2C0; -.
DR jPOST; Q9H2C0; -.
DR MassIVE; Q9H2C0; -.
DR MaxQB; Q9H2C0; -.
DR PaxDb; Q9H2C0; -.
DR PeptideAtlas; Q9H2C0; -.
DR PRIDE; Q9H2C0; -.
DR ProteomicsDB; 80525; -.
DR Antibodypedia; 71668; 135 antibodies from 24 providers.
DR DNASU; 8139; -.
DR Ensembl; ENST00000648994.2; ENSP00000497351.1; ENSG00000261609.8.
DR GeneID; 8139; -.
DR KEGG; hsa:8139; -.
DR MANE-Select; ENST00000648994.2; ENSP00000497351.1; NM_022041.4; NP_071324.1.
DR UCSC; uc002fgo.4; human.
DR CTD; 8139; -.
DR DisGeNET; 8139; -.
DR GeneCards; GAN; -.
DR GeneReviews; GAN; -.
DR HGNC; HGNC:4137; GAN.
DR HPA; ENSG00000261609; Tissue enhanced (skin).
DR MalaCards; GAN; -.
DR MIM; 256850; phenotype.
DR MIM; 605379; gene.
DR neXtProt; NX_Q9H2C0; -.
DR OpenTargets; ENSG00000261609; -.
DR Orphanet; 643; Giant axonal neuropathy.
DR PharmGKB; PA28550; -.
DR VEuPathDB; HostDB:ENSG00000261609; -.
DR eggNOG; KOG4441; Eukaryota.
DR GeneTree; ENSGT00940000155273; -.
DR HOGENOM; CLU_004253_14_2_1; -.
DR InParanoid; Q9H2C0; -.
DR OMA; MCPLYDR; -.
DR OrthoDB; 925701at2759; -.
DR PhylomeDB; Q9H2C0; -.
DR TreeFam; TF329218; -.
DR PathwayCommons; Q9H2C0; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9H2C0; -.
DR SIGNOR; Q9H2C0; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 8139; 16 hits in 1117 CRISPR screens.
DR ChiTaRS; GAN; human.
DR EvolutionaryTrace; Q9H2C0; -.
DR GeneWiki; Gigaxonin; -.
DR GenomeRNAi; 8139; -.
DR Pharos; Q9H2C0; Tbio.
DR PRO; PR:Q9H2C0; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9H2C0; protein.
DR Bgee; ENSG00000261609; Expressed in upper leg skin and 175 other tissues.
DR ExpressionAtlas; Q9H2C0; baseline and differential.
DR Genevisible; Q9H2C0; HS.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR Gene3D; 2.120.10.80; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR017096; BTB-kelch_protein.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR030579; KLHL16.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR24412:SF232; PTHR24412:SF232; 1.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01344; Kelch_1; 3.
DR PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00612; Kelch; 5.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoskeleton; Disease variant; Kelch repeat;
KW Neurodegeneration; Neuropathy; Reference proteome; Repeat; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..597
FT /note="Gigaxonin"
FT /id="PRO_0000119070"
FT DOMAIN 30..99
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 134..236
FT /note="BACK"
FT REPEAT 274..326
FT /note="Kelch 1"
FT REPEAT 327..374
FT /note="Kelch 2"
FT REPEAT 376..421
FT /note="Kelch 3"
FT REPEAT 422..468
FT /note="Kelch 4"
FT REPEAT 470..522
FT /note="Kelch 5"
FT REPEAT 528..574
FT /note="Kelch 6"
FT VARIANT 15
FT /note="R -> S (in GAN1; no effect on binding to TBCB;
FT dbSNP:rs119485093)"
FT /evidence="ECO:0000269|PubMed:11062483,
FT ECO:0000269|PubMed:16303566"
FT /id="VAR_010759"
FT VARIANT 51
FT /note="A -> P (in GAN1; dbSNP:rs750258209)"
FT /evidence="ECO:0000269|PubMed:17578852"
FT /id="VAR_054113"
FT VARIANT 52
FT /note="S -> G (in GAN1; dbSNP:rs1597385719)"
FT /evidence="ECO:0000269|PubMed:11062483"
FT /id="VAR_010760"
FT VARIANT 79
FT /note="S -> L (in GAN1; dbSNP:rs1310137430)"
FT /evidence="ECO:0000269|PubMed:11062483"
FT /id="VAR_010761"
FT VARIANT 82
FT /note="V -> F (in GAN1; no effect on binding to TBCB;
FT dbSNP:rs371054532)"
FT /evidence="ECO:0000269|PubMed:11062483,
FT ECO:0000269|PubMed:16303566"
FT /id="VAR_010762"
FT VARIANT 86
FT /note="I -> F (in GAN1; dbSNP:rs1597400020)"
FT /evidence="ECO:0000269|PubMed:12655563"
FT /id="VAR_015680"
FT VARIANT 89
FT /note="Y -> C (in GAN1; dbSNP:rs1597400024)"
FT /evidence="ECO:0000269|PubMed:17587580"
FT /id="VAR_054114"
FT VARIANT 102
FT /note="I -> T (probable disease-associated variant found in
FT hereditary motor and sensory neuropathy;
FT dbSNP:rs1597401492)"
FT /evidence="ECO:0000269|PubMed:24627108"
FT /id="VAR_073289"
FT VARIANT 138
FT /note="R -> H (in GAN1; dbSNP:rs119485092)"
FT /evidence="ECO:0000269|PubMed:11062483"
FT /id="VAR_010763"
FT VARIANT 195
FT /note="V -> F (in GAN1; dbSNP:rs1432344872)"
FT /evidence="ECO:0000269|PubMed:17587580"
FT /id="VAR_054115"
FT VARIANT 269
FT /note="R -> Q (in GAN1; dbSNP:rs759581558)"
FT /evidence="ECO:0000269|PubMed:11062483,
FT ECO:0000269|PubMed:12655563"
FT /id="VAR_010764"
FT VARIANT 309
FT /note="L -> R (in GAN1; dbSNP:rs1597403384)"
FT /evidence="ECO:0000269|PubMed:11062483"
FT /id="VAR_010765"
FT VARIANT 315
FT /note="P -> L (in GAN1; dbSNP:rs144486241)"
FT /evidence="ECO:0000269|PubMed:17578852"
FT /id="VAR_054116"
FT VARIANT 368
FT /note="G -> R (in GAN1; dbSNP:rs758756818)"
FT /evidence="ECO:0000269|PubMed:12655563,
FT ECO:0000269|PubMed:17587580"
FT /id="VAR_015681"
FT VARIANT 423
FT /note="I -> T (in GAN1; dbSNP:rs119485091)"
FT /evidence="ECO:0000269|PubMed:11971098,
FT ECO:0000269|PubMed:17587580"
FT /id="VAR_015560"
FT VARIANT 438
FT /note="V -> I (probable disease-associated variant found in
FT hereditary motor and sensory neuropathy;
FT dbSNP:rs1246053880)"
FT /evidence="ECO:0000269|PubMed:24627108"
FT /id="VAR_073290"
FT VARIANT 474
FT /note="G -> R (in GAN1; dbSNP:rs1435035575)"
FT /evidence="ECO:0000269|PubMed:17587580"
FT /id="VAR_054117"
FT VARIANT 486
FT /note="E -> K (in GAN1; dbSNP:rs119485088)"
FT /evidence="ECO:0000269|PubMed:11062483"
FT /id="VAR_010757"
FT VARIANT 545
FT /note="R -> C (in GAN1; complete loss of binding to TBCB;
FT dbSNP:rs112201678)"
FT /evidence="ECO:0000269|PubMed:11062483,
FT ECO:0000269|PubMed:16303566"
FT /id="VAR_010766"
FT VARIANT 545
FT /note="R -> H (in GAN1; dbSNP:rs746486469)"
FT /evidence="ECO:0000269|PubMed:17587580"
FT /id="VAR_054118"
FT VARIANT 570
FT /note="C -> Y (in GAN1; dbSNP:rs1597414244)"
FT /evidence="ECO:0000269|PubMed:11062483"
FT /id="VAR_010767"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:2PPI"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:2PPI"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:2PPI"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:2PPI"
FT HELIX 53..61
FT /evidence="ECO:0007829|PDB:2PPI"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2PPI"
FT HELIX 80..90
FT /evidence="ECO:0007829|PDB:2PPI"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:2PPI"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:2PPI"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:2PPI"
FT HELIX 135..143
FT /evidence="ECO:0007829|PDB:3HVE"
FT HELIX 147..164
FT /evidence="ECO:0007829|PDB:3HVE"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:3HVE"
FT HELIX 175..183
FT /evidence="ECO:0007829|PDB:3HVE"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:3HVE"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:3HVE"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:3HVE"
FT HELIX 214..224
FT /evidence="ECO:0007829|PDB:3HVE"
FT HELIX 231..236
FT /evidence="ECO:0007829|PDB:3HVE"
FT HELIX 241..245
FT /evidence="ECO:0007829|PDB:3HVE"
SQ SEQUENCE 597 AA; 67638 MW; 4B6ECFA6849880C7 CRC64;
MAEGSAVSDP QHAARLLRAL SSFREESRFC DAHLVLDGEE IPVQKNILAA ASPYIRTKLN
YNPPKDDGST YKIELEGISV MVMREILDYI FSGQIRLNED TIQDVVQAAD LLLLTDLKTL
CCEFLEGCIA AENCIGIRDF ALHYCLHHVH YLATEYLETH FRDVSSTEEF LELSPQKLKE
VISLEKLNVG NERYVFEAVI RWIAHDTEIR KVHMKDVMSA LWVSGLDSSY LREQMLNEPL
VREIVKECSN IPLSQPQQGE AMLANFKPRG YSECIVTVGG EERVSRKPTA AMRCMCPLYD
PNRQLWIELA PLSMPRINHG VLSAEGFLFV FGGQDENKQT LSSGEKYDPD ANTWTALPPM
NEARHNFGIV EIDGMLYILG GEDGEKELIS MECYDIYSKT WTKQPDLTMV RKIGCYAAMK
KKIYAMGGGS YGKLFESVEC YDPRTQQWTA ICPLKERRFG AVACGVAMEL YVFGGVRSRE
DAQGSEMVTC KSEFYHDEFK RWIYLNDQNL CIPASSSFVY GAVPIGASIY VIGDLDTGTN
YDYVREFKRS TGTWHHTKPL LPSDLRRTGC AALRIANCKL FRLQLQQGLF RIRVHSP
