VPS72_HUMAN
ID VPS72_HUMAN Reviewed; 364 AA.
AC Q15906; A6NLK9; A6PW55; Q53GJ2; Q5U0R4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Vacuolar protein sorting-associated protein 72 homolog;
DE AltName: Full=Protein YL-1;
DE AltName: Full=Transcription factor-like 1;
GN Name=VPS72; Synonyms=TCFL1, YL1;
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] (ISOFORM 1).
RC TISSUE=Fibroblast;
RX PubMed=7702631; DOI=10.1006/bbrc.1995.1433;
RA Horikawa I., Tanaka H., Yuasa Y., Suzuki M., Oshimura M.;
RT "Molecular cloning of a novel human cDNA on chromosome 1q21 and its mouse
RT homolog encoding a nuclear protein with DNA-binding ability.";
RL Biochem. Biophys. Res. Commun. 208:999-1007(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-258 (ISOFORM 2).
RC TISSUE=Embryonic stem cell, and Kidney;
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 [7]
RP IDENTIFICATION IN A NUA4-RELATED COMPLEX.
RX PubMed=14966270; DOI=10.1128/mcb.24.5.1884-1896.2004;
RA Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.;
RT "Structural and functional conservation of the NuA4 histone
RT acetyltransferase complex from yeast to humans.";
RL Mol. Cell. Biol. 24:1884-1896(2004).
RN [8]
RP SUBUNIT.
RX PubMed=15647280; DOI=10.1074/jbc.m500001200;
RA Cai Y., Jin J., Florens L., Swanson S.K., Kusch T., Li B., Workman J.L.,
RA Washburn M.P., Conaway R.C., Conaway J.W.;
RT "The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60 histone
RT acetyltransferase and SRCAP complexes.";
RL J. Biol. Chem. 280:13665-13670(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-129, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, AND IDENTIFICATION BY
RP 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 [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-115, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 6-69 IN COMPLEX WITH H2AZ1 AND
RP H2BC11, FUNCTION, INTERACTION WITH H2AZ1 AND H2BC11, MUTAGENESIS OF
RP 29-PHE--PHE-37 AND 43-ASP--TYR-46, AND SUBCELLULAR LOCATION.
RX PubMed=26974126; DOI=10.1038/nsmb.3189;
RA Latrick C.M., Marek M., Ouararhni K., Papin C., Stoll I., Ignatyeva M.,
RA Obri A., Ennifar E., Dimitrov S., Romier C., Hamiche A.;
RT "Molecular basis and specificity of H2A.Z-H2B recognition and deposition by
RT the histone chaperone YL1.";
RL Nat. Struct. Mol. Biol. 23:309-316(2016).
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-318.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Deposition-and-exchange histone chaperone specific for H2AZ1,
CC specifically chaperones H2AZ1 and deposits it into nucleosomes. As
CC component of the SRCAP complex, mediates the ATP-dependent exchange of
CC histone H2AZ1/H2B dimers for nucleosomal H2A/H2B, leading to
CC transcriptional regulation of selected genes by chromatin remodeling.
CC {ECO:0000269|PubMed:26974126}.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex which
CC contains the catalytic subunit KAT5/TIP60 and the subunits EP400,
CC TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2,
CC ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP,
CC YEATS4/GAS41 and VPS72/YL1. Component of a NuA4-related complex which
CC contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1,
CC RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41.
CC Also part of a multiprotein complex which contains SRCAP and which
CC binds to H2AZ1/H2AZ. Interacts (via N-terminal domain) with heterodimer
CC H2BC11 and H2AZ1 (PubMed:26974126). {ECO:0000269|PubMed:14966270,
CC ECO:0000269|PubMed:15647280, ECO:0000269|PubMed:26974126}.
CC -!- INTERACTION:
CC Q15906; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-399189, EBI-2549423;
CC Q15906; O75031: HSF2BP; NbExp=3; IntAct=EBI-399189, EBI-7116203;
CC Q15906; Q99750: MDFI; NbExp=4; IntAct=EBI-399189, EBI-724076;
CC Q15906; Q9Y265: RUVBL1; NbExp=7; IntAct=EBI-399189, EBI-353675;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:26974126}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15906-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15906-2; Sequence=VSP_047566;
CC -!- SIMILARITY: Belongs to the VPS72/YL1 family. {ECO:0000305}.
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DR EMBL; D43642; BAA07757.1; -; mRNA.
DR EMBL; BT019356; AAV38163.1; -; mRNA.
DR EMBL; BT019357; AAV38164.1; -; mRNA.
DR EMBL; AK222935; BAD96655.1; -; mRNA.
DR EMBL; AK222939; BAD96659.1; -; mRNA.
DR EMBL; AL592424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53462.1; -; Genomic_DNA.
DR EMBL; BC003151; AAH03151.1; -; mRNA.
DR EMBL; CX163016; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS59201.1; -. [Q15906-2]
DR CCDS; CCDS989.1; -. [Q15906-1]
DR PIR; JC4140; JC4140.
DR RefSeq; NP_001258016.1; NM_001271087.1. [Q15906-2]
DR RefSeq; NP_005988.1; NM_005997.2. [Q15906-1]
DR PDB; 5FUG; X-ray; 2.70 A; C/F/I/L=6-69.
DR PDBsum; 5FUG; -.
DR AlphaFoldDB; Q15906; -.
DR SMR; Q15906; -.
DR BioGRID; 112804; 127.
DR ComplexPortal; CPX-974; SRCAP chromatin remodeling complex.
DR ComplexPortal; CPX-978; NuA4 histone acetyltransferase complex.
DR CORUM; Q15906; -.
DR DIP; DIP-31767N; -.
DR IntAct; Q15906; 72.
DR MINT; Q15906; -.
DR STRING; 9606.ENSP00000346464; -.
DR iPTMnet; Q15906; -.
DR PhosphoSitePlus; Q15906; -.
DR BioMuta; VPS72; -.
DR DMDM; 2499159; -.
DR EPD; Q15906; -.
DR jPOST; Q15906; -.
DR MassIVE; Q15906; -.
DR MaxQB; Q15906; -.
DR PaxDb; Q15906; -.
DR PeptideAtlas; Q15906; -.
DR PRIDE; Q15906; -.
DR ProteomicsDB; 1732; -.
DR ProteomicsDB; 60807; -. [Q15906-1]
DR Antibodypedia; 20319; 188 antibodies from 31 providers.
DR DNASU; 6944; -.
DR Ensembl; ENST00000354473.4; ENSP00000346464.4; ENSG00000163159.15. [Q15906-2]
DR Ensembl; ENST00000368892.9; ENSP00000357887.5; ENSG00000163159.15. [Q15906-1]
DR GeneID; 6944; -.
DR KEGG; hsa:6944; -.
DR MANE-Select; ENST00000368892.9; ENSP00000357887.5; NM_005997.3; NP_005988.1.
DR UCSC; uc001exe.3; human. [Q15906-1]
DR CTD; 6944; -.
DR DisGeNET; 6944; -.
DR GeneCards; VPS72; -.
DR HGNC; HGNC:11644; VPS72.
DR HPA; ENSG00000163159; Low tissue specificity.
DR MIM; 600607; gene.
DR neXtProt; NX_Q15906; -.
DR OpenTargets; ENSG00000163159; -.
DR PharmGKB; PA36396; -.
DR VEuPathDB; HostDB:ENSG00000163159; -.
DR eggNOG; KOG2897; Eukaryota.
DR GeneTree; ENSGT00390000017503; -.
DR HOGENOM; CLU_040862_0_0_1; -.
DR InParanoid; Q15906; -.
DR OMA; VNTKAYK; -.
DR OrthoDB; 1468037at2759; -.
DR PhylomeDB; Q15906; -.
DR TreeFam; TF314532; -.
DR PathwayCommons; Q15906; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q15906; -.
DR BioGRID-ORCS; 6944; 315 hits in 1090 CRISPR screens.
DR ChiTaRS; VPS72; human.
DR GeneWiki; VPS72; -.
DR GenomeRNAi; 6944; -.
DR Pharos; Q15906; Tbio.
DR PRO; PR:Q15906; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q15906; protein.
DR Bgee; ENSG00000163159; Expressed in secondary oocyte and 206 other tissues.
DR ExpressionAtlas; Q15906; baseline and differential.
DR Genevisible; Q15906; HS.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:ComplexPortal.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000786; C:nucleosome; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IPI:UniProtKB.
DR GO; GO:0140713; F:histone chaperone activity; IMP:UniProtKB.
DR GO; GO:0045815; P:epigenetic maintenance of chromatin in transcription-competent conformation; IMP:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; IC:ComplexPortal.
DR GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR GO; GO:0043968; P:histone H2A acetylation; IDA:ComplexPortal.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR InterPro; IPR008895; Vps72/YL1.
DR InterPro; IPR013272; Vps72/YL1_C.
DR PANTHER; PTHR13275; PTHR13275; 1.
DR Pfam; PF05764; YL1; 1.
DR Pfam; PF08265; YL1_C; 1.
DR SMART; SM00993; YL1_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..364
FT /note="Vacuolar protein sorting-associated protein 72
FT homolog"
FT /id="PRO_0000066283"
FT DNA_BIND 156..206
FT /evidence="ECO:0000255"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..72
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..352
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 236
FT /note="G -> GSLCFSLSFVLR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047566"
FT VARIANT 318
FT /note="I -> V (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1182821166)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035803"
FT MUTAGEN 29..37
FT /note="FYQTTYGGF->AAQTTAGGA: Highly decreases interaction
FT with H2AZ1 and H2BC11. Abolishes interaction with H2AZ1 and
FT H2BC11 and exchange of H2A for H2AZ1 in nucleosomes; when
FT associated with A-43--46-A."
FT /evidence="ECO:0000269|PubMed:26974126"
FT MUTAGEN 43..46
FT /note="DDEY->ADAA: Almost abolishes interaction with H2AZ1
FT and H2BC11. Abolishes interaction with H2AZ1 and H2BC11 and
FT exchange of H2A for H2AZ1 in nucleosomes; when associated
FT with A-29--37-A."
FT /evidence="ECO:0000269|PubMed:26974126"
FT CONFLICT 30
FT /note="Y -> H (in Ref. 3; BAD96655/BAD96659)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="T -> I (in Ref. 3; BAD96655/BAD96659)"
FT /evidence="ECO:0000305"
FT TURN 11..16
FT /evidence="ECO:0007829|PDB:5FUG"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:5FUG"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:5FUG"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:5FUG"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:5FUG"
SQ SEQUENCE 364 AA; 40594 MW; 0AEB90B62B2BCA4A CRC64;
MSLAGGRAPR KTAGNRLSGL LEAEEEDEFY QTTYGGFTEE SGDDEYQGDQ SDTEDEVDSD
FDIDEGDEPS SDGEAEEPRR KRRVVTKAYK EPLKSLRPRK VNTPAGSSQK AREEKALLPL
ELQDDGSDSR KSMRQSTAEH TRQTFLRVQE RQGQSRRRKG PHCERPLTQE ELLREAKITE
ELNLRSLETY ERLEADKKKQ VHKKRKCPGP IITYHSVTVP LVGEPGPKEE NVDIEGLDPA
PSVSALTPHA GTGPVNPPAR CSRTFITFSD DATFEEWFPQ GRPPKVPVRE VCPVTHRPAL
YRDPVTDIPY ATARAFKIIR EAYKKYITAH GLPPTASALG PGPPPPEPLP GSGPRALRQK
IVIK
