UBXN6_HUMAN
ID UBXN6_HUMAN Reviewed; 441 AA.
AC Q9BZV1; D6W626; Q96AH1; Q96IK9; Q9BZV0;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=UBX domain-containing protein 6 {ECO:0000305};
DE AltName: Full=UBX domain-containing protein 1 {ECO:0000303|PubMed:11342112};
GN Name=UBXN6 {ECO:0000312|HGNC:HGNC:14928};
GN Synonyms=UBXD1 {ECO:0000303|PubMed:11342112, ECO:0000312|HGNC:HGNC:14928},
GN UBXDC2;
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] (ISOFORMS 1 AND 2).
RX PubMed=11342112; DOI=10.1016/s0167-4781(00)00248-7;
RA Carim-Todd L., Escarceller M., Estivill X., Sumoy L.;
RT "Identification and characterization of UBXD1, a novel UBX domain-
RT containing gene on human chromosome 19p13, and its mouse ortholog.";
RL Biochim. Biophys. Acta 1517:298-301(2001).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP INTERACTION WITH VCP; SYVN1 AND HERPUD1, AND SUBCELLULAR LOCATION.
RX PubMed=18656546; DOI=10.1016/j.biocel.2008.06.008;
RA Madsen L., Andersen K.M., Prag S., Moos T., Semple C.A., Seeger M.,
RA Hartmann-Petersen R.;
RT "Ubxd1 is a novel co-factor of the human p97 ATPase.";
RL Int. J. Biochem. Cell Biol. 40:2927-2942(2008).
RN [5]
RP RETRACTION NOTICE OF PUBMED:18656546, AND CAUTION.
RX PubMed=18768758; DOI=10.1091/mbc.e08-01-0067;
RA Zweitzig D.R., Shcherbik N., Haines D.S.;
RT "AAA ATPase p97 and adaptor UBXD1 suppress MDM2 ubiquitination and
RT degradation and promote constitutive p53 turnover.";
RL Mol. Biol. Cell 19:5029-5029(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP INTERACTION WITH VCP.
RX PubMed=19174149; DOI=10.1016/j.bbrc.2009.01.076;
RA Kern M., Fernandez-Saiz V., Schaefer Z., Buchberger A.;
RT "UBXD1 binds p97 through two independent binding sites.";
RL Biochem. Biophys. Res. Commun. 380:303-307(2009).
RN [8]
RP FUNCTION, INTERACTION WITH VCP AND DERL1, SUBCELLULAR LOCATION, AND
RP TOPOLOGY.
RX PubMed=19275885; DOI=10.1016/j.bbrc.2009.03.012;
RA Nagahama M., Ohnishi M., Kawate Y., Matsui T., Miyake H., Yuasa K.,
RA Tani K., Tagaya M., Tsuji A.;
RT "UBXD1 is a VCP-interacting protein that is involved in ER-associated
RT degradation.";
RL Biochem. Biophys. Res. Commun. 382:303-308(2009).
RN [9]
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 [10]
RP INTERACTION WITH VCP, AND VIM MOTIF.
RX PubMed=21896481; DOI=10.1074/jbc.m111.274472;
RA Stapf C., Cartwright E., Bycroft M., Hofmann K., Buchberger A.;
RT "The general definition of the p97/valosin-containing protein (VCP)-
RT interacting motif (VIM) delineates a new family of p97 cofactors.";
RL J. Biol. Chem. 286:38670-38678(2011).
RN [11]
RP FUNCTION, INTERACTION WITH VCP AND CAV1, AND SUBCELLULAR LOCATION.
RX PubMed=21822278; DOI=10.1038/ncb2301;
RA Ritz D., Vuk M., Kirchner P., Bug M., Schuetz S., Hayer A., Bremer S.,
RA Lusk C., Baloh R.H., Lee H., Glatter T., Gstaiger M., Aebersold R.,
RA Weihl C.C., Meyer H.;
RT "Endolysosomal sorting of ubiquitylated caveolin-1 is regulated by VCP and
RT UBXD1 and impaired by VCP disease mutations.";
RL Nat. Cell Biol. 13:1116-1123(2011).
RN [12]
RP INTERACTION WITH LMAN1 AND RAB3GAP1, AND REGION.
RX PubMed=22337587; DOI=10.1074/mcp.m111.016444;
RA Haines D.S., Lee J.E., Beauparlant S.L., Kyle D.B., den Besten W.,
RA Sweredoski M.J., Graham R.L., Hess S., Deshaies R.J.;
RT "Protein interaction profiling of the p97 adaptor UBXD1 points to a role
RT for the complex in modulating ERGIC-53 trafficking.";
RL Mol. Cell. Proteomics 11:M111.016444-M111.016444(2012).
RN [13]
RP FUNCTION.
RX PubMed=23335559; DOI=10.1074/jbc.m112.429076;
RA Kirchner P., Bug M., Meyer H.;
RT "Ubiquitination of the N-terminal region of caveolin-1 regulates endosomal
RT sorting by the VCP/p97 AAA-ATPase.";
RL J. Biol. Chem. 288:7363-7372(2013).
RN [14]
RP INTERACTION WITH VCPKMT.
RX PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
RA Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
RT "A newly uncovered group of distantly related lysine methyltransferases
RT preferentially interact with molecular chaperones to regulate their
RT activity.";
RL PLoS Genet. 9:E1003210-E1003210(2013).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP FUNCTION, AND INTERACTION WITH VCP.
RX PubMed=26475856; DOI=10.1074/jbc.m115.680686;
RA Trusch F., Matena A., Vuk M., Koerver L., Knaevelsrud H., Freemont P.S.,
RA Meyer H., Bayer P.;
RT "The N-terminal Region of the Ubiquitin Regulatory X (UBX) Domain-
RT containing protein 1 (UBXD1) modulates interdomain communication within the
RT valosin-containing protein p97.";
RL J. Biol. Chem. 290:29414-29427(2015).
RN [17]
RP FUNCTION, INTERACTION WITH PLAA; VCP AND YOD1, AND SUBCELLULAR LOCATION.
RX PubMed=27753622; DOI=10.15252/embj.201695148;
RA Papadopoulos C., Kirchner P., Bug M., Grum D., Koerver L., Schulze N.,
RA Poehler R., Dressler A., Fengler S., Arhzaouy K., Lux V., Ehrmann M.,
RA Weihl C.C., Meyer H.;
RT "VCP/p97 cooperates with YOD1, UBXD1 and PLAA to drive clearance of
RT ruptured lysosomes by autophagy.";
RL EMBO J. 36:135-150(2017).
CC -!- FUNCTION: May negatively regulate the ATPase activity of VCP, an ATP-
CC driven segregase that associates with different cofactors to control a
CC wide variety of cellular processes (PubMed:26475856). As a cofactor of
CC VCP, it may play a role in the transport of CAV1 to lysosomes for
CC degradation (PubMed:21822278, PubMed:23335559). It may also play a role
CC in endoplasmic reticulum-associated degradation (ERAD) of misfolded
CC proteins (PubMed:19275885). Together with VCP and other cofactors, it
CC may play a role in macroautophagy, regulating for instance the
CC clearance of damaged lysosomes (PubMed:27753622).
CC {ECO:0000269|PubMed:19275885, ECO:0000269|PubMed:21822278,
CC ECO:0000269|PubMed:23335559, ECO:0000269|PubMed:26475856,
CC ECO:0000269|PubMed:27753622}.
CC -!- SUBUNIT: Interacts with VCP through the PUB domain (via C-terminus) and
CC VIM motif (via N-terminus); the interaction is direct (PubMed:18656546,
CC PubMed:19174149, PubMed:21896481, PubMed:21822278, PubMed:26475856).
CC Forms a ternary complex with CAV1 and VCP (PubMed:21822278). Interacts
CC with SYVN1 (PubMed:18656546). Interacts with HERPUD1 (PubMed:18656546).
CC Interacts with VCPKMT (PubMed:23349634). May interact with DERL1
CC (PubMed:19275885). Interacts with PLAA, VCP and YOD1; may form a
CC complex involved in macroautophagy (PubMed:27753622). Interacts with
CC LMAN1 (PubMed:22337587). {ECO:0000269|PubMed:18656546,
CC ECO:0000269|PubMed:19174149, ECO:0000269|PubMed:19275885,
CC ECO:0000269|PubMed:21822278, ECO:0000269|PubMed:21896481,
CC ECO:0000269|PubMed:22337587, ECO:0000269|PubMed:23349634,
CC ECO:0000269|PubMed:26475856, ECO:0000269|PubMed:27753622}.
CC -!- INTERACTION:
CC Q9BZV1; Q15038: DAZAP2; NbExp=5; IntAct=EBI-1993899, EBI-724310;
CC Q9BZV1; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-1993899, EBI-11978259;
CC Q9BZV1; P43358: MAGEA4; NbExp=4; IntAct=EBI-1993899, EBI-743122;
CC Q9BZV1; Q1RN33: MAGEA4; NbExp=3; IntAct=EBI-1993899, EBI-10194128;
CC Q9BZV1; Q96CS7: PLEKHB2; NbExp=5; IntAct=EBI-1993899, EBI-373552;
CC Q9BZV1; Q92537: SUSD6; NbExp=3; IntAct=EBI-1993899, EBI-2866213;
CC Q9BZV1; Q8NHG7: SVIP; NbExp=3; IntAct=EBI-1993899, EBI-2513231;
CC Q9BZV1; Q9HCM9: TRIM39; NbExp=5; IntAct=EBI-1993899, EBI-739510;
CC Q9BZV1; Q9HCM9-2: TRIM39; NbExp=3; IntAct=EBI-1993899, EBI-11523450;
CC Q9BZV1; Q96LJ8: UBXN10; NbExp=3; IntAct=EBI-1993899, EBI-1993941;
CC Q9BZV1; P68543: UBXN2A; NbExp=3; IntAct=EBI-1993899, EBI-1993668;
CC Q9BZV1; Q14CS0: UBXN2B; NbExp=3; IntAct=EBI-1993899, EBI-1993619;
CC Q9BZV1; P55072: VCP; NbExp=20; IntAct=EBI-1993899, EBI-355164;
CC Q9BZV1; Q5VVQ6: YOD1; NbExp=3; IntAct=EBI-1993899, EBI-2510804;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18656546}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:19275885}. Membrane
CC {ECO:0000269|PubMed:19275885}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19275885}. Nucleus {ECO:0000269|PubMed:18656546}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:18656546}. Early endosome membrane
CC {ECO:0000269|PubMed:21822278}; Peripheral membrane protein
CC {ECO:0000305|PubMed:19275885}. Late endosome membrane
CC {ECO:0000269|PubMed:21822278}; Peripheral membrane protein
CC {ECO:0000305|PubMed:19275885}. Lysosome membrane
CC {ECO:0000269|PubMed:21822278, ECO:0000269|PubMed:27753622}; Peripheral
CC membrane protein {ECO:0000305|PubMed:19275885}. Note=Localizes at the
CC centrosome both in interphase and during mitosis (PubMed:18656546). May
CC be recruited to endosomal and lysosomal membranes as part of a ternary
CC complex with CAV1 and VCP (PubMed:21822278). Recruited to damaged
CC lysosomes decorated with K48-linked ubiquitin chains (PubMed:27753622).
CC {ECO:0000269|PubMed:18656546, ECO:0000269|PubMed:21822278,
CC ECO:0000269|PubMed:27753622}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BZV1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BZV1-2; Sequence=VSP_007453;
CC -!- TISSUE SPECIFICITY: Enhanced expression in testis.
CC -!- DOMAIN: The UBX domain lacks key residues critical for VCP binding.
CC {ECO:0000269|PubMed:21896481}.
CC -!- CAUTION: Was reported to interact with MDM2 and USP7 and to act in a
CC complex with VCP in cooperation with USP7 to promote MDM2
CC deubiquitination and stabilization. However, the corresponding article
CC has been retracted. {ECO:0000305|PubMed:18768758}.
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DR EMBL; AF272893; AAK13257.1; -; mRNA.
DR EMBL; AF272894; AAK13258.1; -; mRNA.
DR EMBL; CH471139; EAW69219.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69222.1; -; Genomic_DNA.
DR EMBL; BC007414; AAH07414.2; -; mRNA.
DR EMBL; BC008288; AAH08288.1; -; mRNA.
DR EMBL; BC017113; AAH17113.1; -; mRNA.
DR CCDS; CCDS12129.1; -. [Q9BZV1-1]
DR CCDS; CCDS54201.1; -. [Q9BZV1-2]
DR RefSeq; NP_001164562.1; NM_001171091.1. [Q9BZV1-2]
DR RefSeq; NP_079517.1; NM_025241.2. [Q9BZV1-1]
DR PDB; 6SAP; NMR; -; A=150-264.
DR PDBsum; 6SAP; -.
DR AlphaFoldDB; Q9BZV1; -.
DR SMR; Q9BZV1; -.
DR BioGRID; 123263; 356.
DR IntAct; Q9BZV1; 27.
DR MINT; Q9BZV1; -.
DR STRING; 9606.ENSP00000301281; -.
DR iPTMnet; Q9BZV1; -.
DR PhosphoSitePlus; Q9BZV1; -.
DR BioMuta; UBXN6; -.
DR DMDM; 30913412; -.
DR EPD; Q9BZV1; -.
DR jPOST; Q9BZV1; -.
DR MassIVE; Q9BZV1; -.
DR MaxQB; Q9BZV1; -.
DR PaxDb; Q9BZV1; -.
DR PeptideAtlas; Q9BZV1; -.
DR PRIDE; Q9BZV1; -.
DR ProteomicsDB; 79904; -. [Q9BZV1-1]
DR ProteomicsDB; 79905; -. [Q9BZV1-2]
DR Antibodypedia; 42425; 178 antibodies from 26 providers.
DR DNASU; 80700; -.
DR Ensembl; ENST00000301281.11; ENSP00000301281.5; ENSG00000167671.12. [Q9BZV1-1]
DR Ensembl; ENST00000394765.7; ENSP00000378246.2; ENSG00000167671.12. [Q9BZV1-2]
DR GeneID; 80700; -.
DR KEGG; hsa:80700; -.
DR MANE-Select; ENST00000301281.11; ENSP00000301281.5; NM_025241.3; NP_079517.1.
DR UCSC; uc002mam.3; human. [Q9BZV1-1]
DR CTD; 80700; -.
DR DisGeNET; 80700; -.
DR GeneCards; UBXN6; -.
DR HGNC; HGNC:14928; UBXN6.
DR HPA; ENSG00000167671; Low tissue specificity.
DR MIM; 611946; gene.
DR neXtProt; NX_Q9BZV1; -.
DR OpenTargets; ENSG00000167671; -.
DR PharmGKB; PA162408446; -.
DR VEuPathDB; HostDB:ENSG00000167671; -.
DR eggNOG; KOG2699; Eukaryota.
DR GeneTree; ENSGT00940000157273; -.
DR HOGENOM; CLU_033280_0_0_1; -.
DR InParanoid; Q9BZV1; -.
DR OMA; FFRCPMI; -.
DR OrthoDB; 963177at2759; -.
DR PhylomeDB; Q9BZV1; -.
DR TreeFam; TF314617; -.
DR PathwayCommons; Q9BZV1; -.
DR SignaLink; Q9BZV1; -.
DR BioGRID-ORCS; 80700; 17 hits in 1085 CRISPR screens.
DR ChiTaRS; UBXN6; human.
DR GeneWiki; UBXN6; -.
DR GenomeRNAi; 80700; -.
DR Pharos; Q9BZV1; Tbio.
DR PRO; PR:Q9BZV1; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BZV1; protein.
DR Bgee; ENSG00000167671; Expressed in right testis and 196 other tissues.
DR ExpressionAtlas; Q9BZV1; baseline and differential.
DR Genevisible; Q9BZV1; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:CACAO.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0032510; P:endosome to lysosome transport via multivesicular body sorting pathway; IMP:UniProtKB.
DR GO; GO:0036503; P:ERAD pathway; IMP:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; IMP:UniProtKB.
DR CDD; cd10460; PUB_UBXD1; 1.
DR InterPro; IPR036339; PUB-like_dom_sf.
DR InterPro; IPR018997; PUB_domain.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR InterPro; IPR042774; UBXN6_PUB.
DR Pfam; PF09409; PUB; 1.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF143503; SSF143503; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton; Endosome;
KW Lysosome; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..441
FT /note="UBX domain-containing protein 6"
FT /id="PRO_0000211025"
FT DOMAIN 175..244
FT /note="PUB"
FT /evidence="ECO:0000255"
FT DOMAIN 332..408
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 1..10
FT /note="Mediates interaction with LMAN1"
FT /evidence="ECO:0000269|PubMed:22337587"
FT REGION 13..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..63
FT /note="VCP/p97-interacting motif (VIM)"
FT /evidence="ECO:0000269|PubMed:21896481"
FT REGION 87..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11342112,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007453"
FT VARIANT 31
FT /note="A -> T (in dbSNP:rs1127888)"
FT /id="VAR_061924"
FT VARIANT 425
FT /note="P -> L (in dbSNP:rs35436704)"
FT /id="VAR_047821"
FT HELIX 153..164
FT /evidence="ECO:0007829|PDB:6SAP"
FT HELIX 168..187
FT /evidence="ECO:0007829|PDB:6SAP"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:6SAP"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:6SAP"
FT HELIX 202..206
FT /evidence="ECO:0007829|PDB:6SAP"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:6SAP"
FT HELIX 214..220
FT /evidence="ECO:0007829|PDB:6SAP"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:6SAP"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:6SAP"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:6SAP"
FT HELIX 250..261
FT /evidence="ECO:0007829|PDB:6SAP"
SQ SEQUENCE 441 AA; 49754 MW; FC06E6ADA1A1036C CRC64;
MKKFFQEFKA DIKFKSAGPG QKLKESVGEK AHKEKPNQPA PRPPRQGPTN EAQMAAAAAL
ARLEQKQSRA WGPTSQDTIR NQVRKELQAE ATVSGSPEAP GTNVVSEPRE EGSAHLAVPG
VYFTCPLTGA TLRKDQRDAC IKEAILLHFS TDPVAASIMK IYTFNKDQDR VKLGVDTIAK
YLDNIHLHPE EEKYRKIKLQ NKVFQERINC LEGTHEFFEA IGFQKVLLPA QDQEDPEEFY
VLSETTLAQP QSLERHKEQL LAAEPVRAKL DRQRRVFQPS PLASQFELPG DFFNLTAEEI
KREQRLRSEA VERLSVLRTK AMREKEEQRG LRKYNYTLLR VRLPDGCLLQ GTFYARERLG
AVYGFVREAL QSDWLPFELL ASGGQKLSED ENLALNECGL VPSALLTFSW DMAVLEDIKA
AGAEPDSILK PELLSAIEKL L
