VPS4B_MOUSE
ID VPS4B_MOUSE Reviewed; 444 AA.
AC P46467; Q91W22; Q9R1C9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Vacuolar protein sorting-associated protein 4B {ECO:0000305};
DE EC=3.6.4.6;
DE AltName: Full=Suppressor of K(+) transport growth defect 1;
DE Short=Protein SKD1;
GN Name=Vps4b {ECO:0000312|MGI:MGI:1100499}; Synonyms=Skd1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=8082782; DOI=10.1016/0014-5793(94)00879-5;
RA Perier F., Coulter K.L., Liang H., Radeke C.M., Gaber R.F.,
RA Vandenberg C.A.;
RT "Identification of a novel mammalian member of the NSF/CDC48p/Pas1p/TBP-1
RT family through heterologous expression in yeast.";
RL FEBS Lett. 351:286-290(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=10393249; DOI=10.1016/s0378-1119(99)00163-8;
RA Scheuring S., Bodor O., Rohricht R.A., Muller S., Beyer A., Kohrer K.;
RT "Cloning, characterisation, and functional expression of the Mus musculus
RT SKD1 gene in yeast demonstrates that the mouse SKD1 and the yeast VPS4
RT genes are orthologues and involved in intracellular protein trafficking.";
RL Gene 234:149-159(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INTERACTION WITH VPS4A, AND MUTAGENESIS OF GLU-235.
RX PubMed=12594041; DOI=10.1016/s0378-1119(02)01205-2;
RA Beyer A., Scheuring S., Mueller S., Mincheva A., Lichter P., Koehrer K.;
RT "Comparative sequence and expression analyses of four mammalian VPS4
RT genes.";
RL Gene 305:47-59(2003).
RN [5]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-180 AND GLU-235.
RX PubMed=10637304; DOI=10.1091/mbc.11.1.227;
RA Bishop N., Woodman P.;
RT "ATPase-defective mammalian VPS4 localizes to aberrant endosomes and
RT impairs cholesterol trafficking.";
RL Mol. Biol. Cell 11:227-239(2000).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF GLU-235.
RX PubMed=10679028; DOI=10.1091/mbc.11.2.747;
RA Yoshimori T., Yamagata F., Yamamoto A., Mizushima N., Kabeya Y., Nara A.,
RA Miwako I., Ohashi M., Ohsumi M., Ohsumi Y.;
RT "The mouse SKD1, a homologue of yeast Vps4p, is required for normal
RT endosomal trafficking and morphology in mammalian cells.";
RL Mol. Biol. Cell 11:747-763(2000).
RN [7]
RP INTERACTION WITH CHMP2A.
RX PubMed=15173323; DOI=10.1242/jcs.01170;
RA Fujita H., Umezuki Y., Imamura K., Ishikawa D., Uchimura S., Nara A.,
RA Yoshimori T., Hayashizaki Y., Kawai J., Ishidoh K., Tanaka Y., Himeno M.;
RT "Mammalian class E Vps proteins, SBP1 and mVps2/CHMP2A, interact with and
RT regulate the function of an AAA-ATPase SKD1/Vps4B.";
RL J. Cell Sci. 117:2997-3009(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 123-444, SUBUNIT, AND MUTAGENESIS
RP OF GLU-235 AND 290-ARG-ARG-291.
RX PubMed=18796009; DOI=10.1111/j.1600-0854.2008.00831.x;
RA Inoue M., Kamikubo H., Kataoka M., Kato R., Yoshimori T., Wakatsuki S.,
RA Kawasaki M.;
RT "Nucleotide-dependent conformational changes and assembly of the AAA ATPase
RT SKD1/VPS4B.";
RL Traffic 9:2180-2189(2008).
CC -!- FUNCTION: Involved in late steps of the endosomal multivesicular bodies
CC (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and
CC catalyzes their disassembly, possibly in combination with membrane
CC fission. Redistributes the ESCRT-III components to the cytoplasm for
CC further rounds of MVB sorting. MVBs contain intraluminal vesicles
CC (ILVs) that are generated by invagination and scission from the
CC limiting membrane of the endosome and mostly are delivered to lysosomes
CC enabling degradation of membrane proteins, such as stimulated growth
CC factor receptors, lysosomal enzymes and lipids. VPS4A/B are required
CC for the exosomal release of SDCBP, CD63 and syndecan (By similarity).
CC {ECO:0000250|UniProtKB:O75351, ECO:0000269|PubMed:10393249,
CC ECO:0000269|PubMed:10679028}.
CC -!- FUNCTION: (Microbial infection) In conjunction with the ESCRT machinery
CC also appears to function in topologically equivalent membrane fission
CC events, such as the terminal stages of cytokinesis and enveloped virus
CC budding (lentiviruses). {ECO:0000250|UniProtKB:O75351}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6;
CC -!- SUBUNIT: Proposed to be monomeric or homodimeric in nucleotide-free
CC form and to oligomerize upon binding to ATP to form two stacked
CC hexameric or heptameric rings with a central pore through which ESCRT-
CC III substrates are translocated in an ATP-dependent manner. In vitro,
CC associates on the inside of a helical tubular structure formed by a
CC CHMP2A-CHMP3 polymer. Interacts with CHMP1A, CHMP1B, CHMP4B and CHMP6.
CC Interacts with CHMP2A (PubMed:15173323). Interacts with VPS4A; the
CC interaction suggests a heteromeric assembly with VPS4A
CC (PubMed:12594041). Interacts with VTA1 (By similarity).
CC {ECO:0000250|UniProtKB:O75351, ECO:0000269|PubMed:12594041,
CC ECO:0000269|PubMed:15173323}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000269|PubMed:12594041}; Peripheral membrane protein
CC {ECO:0000305}. Note=Membrane-associated in the prevacuolar endosomal
CC compartment.
CC -!- TISSUE SPECIFICITY: High level expression seen in the kidney. It is
CC also expressed in the heart, brain, spleen, lung, liver, skeletal
CC muscle, and testis. {ECO:0000269|PubMed:12594041,
CC ECO:0000269|PubMed:8082782}.
CC -!- DOMAIN: The MIT domain serves as an adapter for ESCRT-III proteins. It
CC forms an asymmetric three-helix bundle that binds amphipathic MIM (MIT
CC interacting motif) helices along the groove between MIT helices 2 and 3
CC present in a subset of ESCRT-III proteins thus establishing the
CC canonical MIM-MIT interaction. In an extended conformation along the
CC groove between helices 1 and 3, also binds to a type-2 MIT interacting
CC motif (MIM2). {ECO:0000250|UniProtKB:O75351}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; U10119; AAA50497.1; -; mRNA.
DR EMBL; AF134119; AAD47570.1; -; Genomic_DNA.
DR EMBL; BC003799; AAH03799.1; -; mRNA.
DR CCDS; CCDS15211.1; -.
DR PIR; S48696; S48696.
DR RefSeq; NP_033216.2; NM_009190.2.
DR PDB; 2ZAM; X-ray; 3.50 A; A=1-444.
DR PDB; 2ZAN; X-ray; 3.00 A; A=1-444.
DR PDB; 2ZAO; X-ray; 3.20 A; A=1-444.
DR PDBsum; 2ZAM; -.
DR PDBsum; 2ZAN; -.
DR PDBsum; 2ZAO; -.
DR AlphaFoldDB; P46467; -.
DR SMR; P46467; -.
DR BioGRID; 203266; 65.
DR ComplexPortal; CPX-340; VPS4A/B complex.
DR IntAct; P46467; 59.
DR MINT; P46467; -.
DR STRING; 10090.ENSMUSP00000092230; -.
DR iPTMnet; P46467; -.
DR PhosphoSitePlus; P46467; -.
DR EPD; P46467; -.
DR jPOST; P46467; -.
DR PaxDb; P46467; -.
DR PeptideAtlas; P46467; -.
DR PRIDE; P46467; -.
DR ProteomicsDB; 275184; -.
DR Antibodypedia; 23094; 195 antibodies from 30 providers.
DR DNASU; 20479; -.
DR Ensembl; ENSMUST00000094646; ENSMUSP00000092230; ENSMUSG00000009907.
DR Ensembl; ENSMUST00000112736; ENSMUSP00000108356; ENSMUSG00000009907.
DR GeneID; 20479; -.
DR KEGG; mmu:20479; -.
DR UCSC; uc007cgz.2; mouse.
DR CTD; 9525; -.
DR MGI; MGI:1100499; Vps4b.
DR VEuPathDB; HostDB:ENSMUSG00000009907; -.
DR eggNOG; KOG0739; Eukaryota.
DR GeneTree; ENSGT00940000154973; -.
DR HOGENOM; CLU_000688_21_2_1; -.
DR InParanoid; P46467; -.
DR OMA; AVQYFIH; -.
DR OrthoDB; 787710at2759; -.
DR PhylomeDB; P46467; -.
DR TreeFam; TF105012; -.
DR BRENDA; 3.6.4.6; 3474.
DR Reactome; R-MMU-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR BioGRID-ORCS; 20479; 29 hits in 72 CRISPR screens.
DR ChiTaRS; Vps4b; mouse.
DR EvolutionaryTrace; P46467; -.
DR PRO; PR:P46467; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P46467; protein.
DR Bgee; ENSMUSG00000009907; Expressed in conjunctival fornix and 257 other tissues.
DR ExpressionAtlas; P46467; baseline and differential.
DR Genevisible; P46467; MM.
DR GO; GO:1904949; C:ATPase complex; IC:ComplexPortal.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; ISO:MGI.
DR GO; GO:0090543; C:Flemming body; ISO:MGI.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IC:ComplexPortal.
DR GO; GO:0005643; C:nuclear pore; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0000922; C:spindle pole; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0097352; P:autophagosome maturation; IC:ComplexPortal.
DR GO; GO:0006914; P:autophagy; IC:ComplexPortal.
DR GO; GO:0030301; P:cholesterol transport; IMP:MGI.
DR GO; GO:0016197; P:endosomal transport; ISO:MGI.
DR GO; GO:0007032; P:endosome organization; IMP:MGI.
DR GO; GO:0032510; P:endosome to lysosome transport via multivesicular body sorting pathway; ISO:MGI.
DR GO; GO:1904903; P:ESCRT III complex disassembly; ISO:MGI.
DR GO; GO:0061738; P:late endosomal microautophagy; IMP:ParkinsonsUK-UCL.
DR GO; GO:0061764; P:late endosome to lysosome transport via multivesicular body sorting pathway; IC:ComplexPortal.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0061952; P:midbody abscission; ISO:MGI.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISO:MGI.
DR GO; GO:0036258; P:multivesicular body assembly; IMP:ParkinsonsUK-UCL.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IC:ComplexPortal.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:1903542; P:negative regulation of exosomal secretion; ISO:MGI.
DR GO; GO:0031468; P:nuclear membrane reassembly; IC:ComplexPortal.
DR GO; GO:0006997; P:nucleus organization; ISO:MGI.
DR GO; GO:0001778; P:plasma membrane repair; IC:ComplexPortal.
DR GO; GO:1903724; P:positive regulation of centriole elongation; ISO:MGI.
DR GO; GO:1903543; P:positive regulation of exosomal secretion; ISO:MGI.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0006813; P:potassium ion transport; IDA:MGI.
DR GO; GO:0051261; P:protein depolymerization; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0010824; P:regulation of centrosome duplication; ISO:MGI.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; ISO:MGI.
DR GO; GO:0033993; P:response to lipid; ISO:MGI.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISO:MGI.
DR GO; GO:0090611; P:ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway; ISO:MGI.
DR GO; GO:0046761; P:viral budding from plasma membrane; IMP:UniProtKB.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; ISO:MGI.
DR CDD; cd02678; MIT_VPS4; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR031255; VPS4.
DR InterPro; IPR015415; Vps4_C.
DR InterPro; IPR045253; VPS4_MIT.
DR PANTHER; PTHR23074:SF72; PTHR23074:SF72; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF04212; MIT; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00745; MIT; 1.
DR SUPFAM; SSF116846; SSF116846; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Coiled coil;
KW Endosome; Hydrolase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..444
FT /note="Vacuolar protein sorting-associated protein 4B"
FT /id="PRO_0000084768"
FT DOMAIN 4..82
FT /note="MIT"
FT REGION 77..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 19..82
FT /evidence="ECO:0000255"
FT COMPBIAS 77..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 174..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75351"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75351"
FT MUTAGEN 180
FT /note="K->Q: Defective in ATP-binding. Causes membrane
FT association. Induces vacuolation of endosomal compartments
FT and impairs cholesterol sorting."
FT /evidence="ECO:0000269|PubMed:10637304"
FT MUTAGEN 235
FT /note="E->Q: Defective in ATP-hydrolysis. Causes membrane-
FT association. Induces vacuolation of endosomal compartments
FT and impairs cholesterol and protein sorting. Increased
FT perinuclear localization."
FT /evidence="ECO:0000269|PubMed:10637304,
FT ECO:0000269|PubMed:10679028, ECO:0000269|PubMed:12594041,
FT ECO:0000269|PubMed:18796009"
FT MUTAGEN 290..291
FT /note="RR->AA: Abolishes ATP-dependent oligomerization."
FT /evidence="ECO:0000269|PubMed:18796009"
FT CONFLICT 90
FT /note="E -> A (in Ref. 1; AAA50497)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="A -> V (in Ref. 1; AAA50497)"
FT /evidence="ECO:0000305"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:2ZAN"
FT HELIX 140..150
FT /evidence="ECO:0007829|PDB:2ZAN"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:2ZAN"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:2ZAN"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:2ZAN"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:2ZAN"
FT HELIX 180..190
FT /evidence="ECO:0007829|PDB:2ZAN"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:2ZAN"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:2ZAM"
FT HELIX 216..225
FT /evidence="ECO:0007829|PDB:2ZAN"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:2ZAN"
FT TURN 236..239
FT /evidence="ECO:0007829|PDB:2ZAN"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:2ZAN"
FT HELIX 252..259
FT /evidence="ECO:0007829|PDB:2ZAN"
FT TURN 260..263
FT /evidence="ECO:0007829|PDB:2ZAN"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:2ZAM"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:2ZAN"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:2ZAN"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:2ZAN"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:2ZAN"
FT HELIX 303..314
FT /evidence="ECO:0007829|PDB:2ZAN"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:2ZAO"
FT HELIX 323..332
FT /evidence="ECO:0007829|PDB:2ZAN"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:2ZAN"
FT HELIX 338..349
FT /evidence="ECO:0007829|PDB:2ZAN"
FT HELIX 351..358
FT /evidence="ECO:0007829|PDB:2ZAN"
FT STRAND 360..365
FT /evidence="ECO:0007829|PDB:2ZAN"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:2ZAO"
FT STRAND 380..384
FT /evidence="ECO:0007829|PDB:2ZAN"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:2ZAO"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:2ZAN"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:2ZAN"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:2ZAO"
FT HELIX 411..419
FT /evidence="ECO:0007829|PDB:2ZAN"
FT HELIX 427..436
FT /evidence="ECO:0007829|PDB:2ZAN"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:2ZAN"
SQ SEQUENCE 444 AA; 49419 MW; AA95B607DF8706A1 CRC64;
MASTNTNLQK AIDLASKAAQ EDKAGNYEEA LQLYQHAVQY FLHVVKYEAQ GDKAKQSIRA
KCTEYLDRAE KLKEYLKKKE KKPQKPVKEE QSGPVDEKGN DSDGEAESDD PEKKKLQNQL
QGAIVIERPN VKWSDVAGLE GAKEALKEAV ILPIKFPHLF TGKRTPWRGI LLFGPPGTGK
SYLAKAVATE ANNSTFFSIS SSDLVSKWLG ESEKLVKNLF QLARENKPSI IFIDEIDSLC
GSRSENESEA ARRIKTEFLV QMQGVGVDND GILVLGATNI PWVLDSAIRR RFEKRIYIPL
PEAHARAAMF RLHLGSTQNS LTEADFQELG RKTDGYSGAD ISIIVRDALM QPVRKVQSAT
HFKKVRGPSR ADPNCIVNDL LTPCSPGDPG AIEMTWMDVP GDKLLEPVVS MWDMLRSLSS
TKPTVNEQDL LKLKKFTEDF GQEG
