HAP40_HUMAN
ID HAP40_HUMAN Reviewed; 371 AA.
AC P23610; Q5HY66; Q8IXP3;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=40-kDa huntingtin-associated protein {ECO:0000303|PubMed:16476778};
DE Short=HAP40 {ECO:0000303|PubMed:16476778};
DE AltName: Full=CpG island protein;
DE AltName: Full=Factor VIII intron 22 protein;
GN Name=F8A1;
GN and
GN Name=F8A2;
GN and
GN Name=F8A3;
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 [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=2110545; DOI=10.1016/0888-7543(90)90512-s;
RA Levinson B., Kenwrick S., Lakich D., Hammonds G. Jr., Gitschier J.;
RT "A transcribed gene in an intron of the human factor VIII gene.";
RL Genomics 7:1-11(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Bagnall R.D., Green P.M., Giannelli F.;
RT "Gene conversion and evolution of Xq28 duplicons involved in recurring
RT inversions causing severe haemophilia A.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood, and Brain;
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 [6]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16476778; DOI=10.1083/jcb.200509091;
RA Pal A., Severin F., Lommer B., Shevchenko A., Zerial M.;
RT "Huntingtin-HAP40 complex is a novel Rab5 effector that regulates early
RT endosome motility and is up-regulated in Huntington's disease.";
RL J. Cell Biol. 172:605-618(2006).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP PROBABLE ROLE IN HUNTINGTON'S DISEASE.
RX PubMed=27815841; DOI=10.1007/s12035-016-0247-y;
RA Huang Z.N., Her L.S.;
RT "The Ubiquitin Receptor ADRM1 Modulates HAP40-Induced Proteasome
RT Activity.";
RL Mol. Neurobiol. 54:7382-7400(2017).
RN [13]
RP PROBABLE ROLE IN HUNTINGTON'S DISEASE.
RX PubMed=29209146; DOI=10.7150/ijbs.20742;
RA Huang Z.N., Chung H.M., Fang S.C., Her L.S.;
RT "Adhesion Regulating Molecule 1 Mediates HAP40 Overexpression-Induced
RT Mitochondrial Defects.";
RL Int. J. Biol. Sci. 13:1420-1437(2017).
RN [14] {ECO:0007744|PDB:6EZ8}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS) IN COMPLEX WITH HTT, AND
RP INTERACTION WITH HTT.
RX PubMed=29466333; DOI=10.1038/nature25502;
RA Guo Q., Huang B., Cheng J., Seefelder M., Engler T., Pfeifer G., Oeckl P.,
RA Otto M., Moser F., Maurer M., Pautsch A., Baumeister W.,
RA Fernandez-Busnadiego R., Kochanek S.;
RT "The cryo-electron microscopy structure of huntingtin.";
RL Nature 555:117-120(2018).
CC -!- FUNCTION: RAB5A effector molecule that is involved in vesicular
CC trafficking of early endosomes (PubMed:16476778). Mediates the
CC recruitment of HTT by RAB5A onto early endosomes. The HTT-
CC F8A1/F8A2/F8A3-RAB5A complex stimulates early endosomal interaction
CC with actin filaments and inhibits interaction with microtubules,
CC leading to the reduction of endosome motility (PubMed:16476778).
CC {ECO:0000269|PubMed:16476778}.
CC -!- SUBUNIT: Interacts with HTT (via C-terminus) (PubMed:29466333).
CC Interacts with RAB5A (By similarity). Found in a complex with
CC F8A1/F8A2/F8A3, HTT and RAB5A; mediates the recruitment of HTT by RAB5A
CC onto early endosomes (By similarity). {ECO:0000250|UniProtKB:M0RDU0,
CC ECO:0000269|PubMed:29466333}.
CC -!- INTERACTION:
CC P23610; P42858: HTT; NbExp=3; IntAct=EBI-5663973, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16476778}. Nucleus
CC {ECO:0000269|PubMed:16476778}. Early endosome
CC {ECO:0000269|PubMed:16476778}. Nucleus, nuclear body
CC {ECO:0000250|UniProtKB:Q00558}. Note=Diffuse presence in the cytoplasm
CC and accumulation in the nucleus (PubMed:16476778). In absence of HTT,
CC F8A1/F8A2/F8A3 is concentred in cytoplasm (By similarity). Colocalized
CC with HTT in endosomes (PubMed:16476778). In neuron found in
CC intranuclear structures, the intranuclear rodlets (INRs), also known as
CC rodlets of Roncoroni, in association with ubiquitin (By similarity).
CC {ECO:0000250|UniProtKB:Q00558, ECO:0000269|PubMed:16476778}.
CC -!- TISSUE SPECIFICITY: Produced abundantly in a wide variety of cell
CC types.
CC -!- DISEASE: Note=Up-regulated in brain tissue from patients affected by
CC Huntington's disease (at protein level) (PubMed:16476778). In a
CC Huntington's disease mouse model overexpression of F8A1/F8A2/F8A3
CC impairs proteasome activity leading to the accumulation of mutant HTT
CC and causes defective mitochondrial functions (PubMed:27815841,
CC PubMed:29209146). {ECO:0000269|PubMed:16476778,
CC ECO:0000269|PubMed:27815841, ECO:0000269|PubMed:29209146}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35713.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M34677; AAA35713.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AY619999; AAT44606.1; -; Genomic_DNA.
DR EMBL; AY620000; AAT44607.1; -; Genomic_DNA.
DR EMBL; AY620001; AAT44608.1; -; Genomic_DNA.
DR EMBL; BX276110; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX682237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX842559; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471172; EAW72648.1; -; Genomic_DNA.
DR EMBL; BC039693; AAH39693.1; -; mRNA.
DR EMBL; BC071963; AAH71963.1; -; mRNA.
DR CCDS; CCDS35459.1; -.
DR CCDS; CCDS35462.1; -.
DR CCDS; CCDS35463.1; -.
DR PIR; B42832; B42832.
DR RefSeq; NP_001007524.1; NM_001007523.1.
DR RefSeq; NP_001007525.1; NM_001007524.1.
DR RefSeq; NP_036283.2; NM_012151.3.
DR PDB; 6EZ8; EM; 4.00 A; B=1-371.
DR PDB; 6X9O; EM; 2.60 A; B=1-371.
DR PDB; 7DXJ; EM; 3.60 A; B=1-371.
DR PDB; 7DXK; EM; 4.10 A; B=1-371.
DR PDBsum; 6EZ8; -.
DR PDBsum; 6X9O; -.
DR PDBsum; 7DXJ; -.
DR PDBsum; 7DXK; -.
DR AlphaFoldDB; P23610; -.
DR SMR; P23610; -.
DR BioGRID; 113884; 10.
DR BioGRID; 138884; 4.
DR IntAct; P23610; 5.
DR STRING; 9606.ENSP00000358518; -.
DR iPTMnet; P23610; -.
DR PhosphoSitePlus; P23610; -.
DR BioMuta; F8A2; -.
DR DMDM; 55977780; -.
DR EPD; P23610; -.
DR jPOST; P23610; -.
DR MassIVE; P23610; -.
DR MaxQB; P23610; -.
DR PaxDb; P23610; -.
DR PeptideAtlas; P23610; -.
DR PRIDE; P23610; -.
DR ProteomicsDB; 54136; -.
DR Antibodypedia; 72328; 65 antibodies from 15 providers.
DR Antibodypedia; 74674; 36 antibodies from 8 providers.
DR Antibodypedia; 77183; 1 antibodies from 1 providers.
DR DNASU; 8263; -.
DR Ensembl; ENST00000369505.5; ENSP00000358518.3; ENSG00000288709.1.
DR Ensembl; ENST00000610495.2; ENSP00000479624.1; ENSG00000288722.1.
DR Ensembl; ENST00000622749.2; ENSP00000477530.2; ENSG00000277150.2.
DR GeneID; 474383; -.
DR GeneID; 474384; -.
DR GeneID; 8263; -.
DR KEGG; hsa:474383; -.
DR KEGG; hsa:474384; -.
DR KEGG; hsa:8263; -.
DR MANE-Select; ENST00000369505.5; ENSP00000358518.3; NM_001007523.2; NP_001007524.1.
DR MANE-Select; ENST00000610495.2; ENSP00000479624.1; NM_012151.4; NP_036283.2.
DR MANE-Select; ENST00000622749.2; ENSP00000477530.2; NM_001007524.2; NP_001007525.1.
DR UCSC; uc004fmv.4; human.
DR CTD; 474383; -.
DR CTD; 474384; -.
DR CTD; 8263; -.
DR DisGeNET; 474383; -.
DR DisGeNET; 474384; -.
DR DisGeNET; 8263; -.
DR GeneCards; F8A1; -.
DR GeneCards; F8A2; -.
DR GeneCards; F8A3; -.
DR HGNC; HGNC:3547; F8A1.
DR HGNC; HGNC:31849; F8A2.
DR HGNC; HGNC:31850; F8A3.
DR HPA; ENSG00000274791; Tissue enriched (brain).
DR HPA; ENSG00000277150; Low tissue specificity.
DR HPA; ENSG00000277203; Low tissue specificity.
DR MIM; 305423; gene.
DR neXtProt; NX_P23610; -.
DR OpenTargets; ENSG00000277150; -.
DR PharmGKB; PA27953; -.
DR VEuPathDB; HostDB:ENSG00000274791; -.
DR VEuPathDB; HostDB:ENSG00000277150; -.
DR VEuPathDB; HostDB:ENSG00000277203; -.
DR eggNOG; ENOG502QQQW; Eukaryota.
DR GeneTree; ENSGT00390000016992; -.
DR HOGENOM; CLU_076185_0_0_1; -.
DR InParanoid; P23610; -.
DR OMA; YCWEAPE; -.
DR OrthoDB; 1141704at2759; -.
DR PhylomeDB; P23610; -.
DR TreeFam; TF313929; -.
DR PathwayCommons; P23610; -.
DR SignaLink; P23610; -.
DR BioGRID-ORCS; 474383; 21 hits in 160 CRISPR screens.
DR BioGRID-ORCS; 474384; 90 hits in 579 CRISPR screens.
DR BioGRID-ORCS; 8263; 27 hits in 228 CRISPR screens.
DR ChiTaRS; F8A1; human.
DR ChiTaRS; F8A3; human.
DR GeneWiki; F8A1; -.
DR Pharos; P23610; Tbio.
DR PRO; PR:P23610; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P23610; protein.
DR Bgee; ENSG00000277150; Expressed in stromal cell of endometrium and 94 other tissues.
DR Genevisible; P23610; HS.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IMP:UniProtKB.
DR GO; GO:0099518; P:vesicle cytoskeletal trafficking; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR039494; F8A.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR16797; PTHR16797; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Endosome; Nucleus;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..371
FT /note="40-kDa huntingtin-associated protein"
FT /id="PRO_0000087159"
FT REGION 213..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 34..36
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q00558"
FT COMPBIAS 219..241
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CONFLICT 105..107
FT /note="RQR -> PA (in Ref. 1; AAA35713)"
FT /evidence="ECO:0000305"
FT HELIX 84..105
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 117..135
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 138..154
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 158..172
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 177..193
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 197..214
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 261..280
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 289..297
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 316..330
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 334..344
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 345..347
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 350..364
FT /evidence="ECO:0007829|PDB:6X9O"
SQ SEQUENCE 371 AA; 39103 MW; 0E230A1978FAB59D CRC64;
MAAAAAGLGG GGAGPGPEAG DFLARYRLVS NKLKKRFLRK PNVAEAGEQF GQLGRELRAQ
ECLPYAAWCQ LAVARCQQAL FHGPGEALAL TEAARLFLRQ ERDARQRLVC PAAYGEPLQA
AASALGAAVR LHLELGQPAA AAALCLELAA ALRDLGQPAA AAGHFQRAAQ LQLPQLPLAA
LQALGEAASC QLLARDYTGA LAVFTRMQRL AREHGSHPVQ SLPPPPPPAP QPGPGATPAL
PAALLPPNSG SAAPSPAALG AFSDVLVRCE VSRVLLLLLL QPPPAKLLPE HAQTLEKYSW
EAFDSHGQES SGQLPEELFL LLQSLVMATH EKDTEAIKSL QVEMWPLLTA EQNHLLHLVL
QETISPSGQG V
