DOP2_HUMAN
ID DOP2_HUMAN Reviewed; 2298 AA.
AC Q9Y3R5; D3DSG5; Q6PJQ7; Q9UEZ3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 5.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Protein dopey-2;
GN Name=DOP1B {ECO:0000312|HGNC:HGNC:1291};
GN Synonyms=C21orf5, DOPEY2 {ECO:0000303|PubMed:30213940,
GN ECO:0000312|HGNC:HGNC:1291}, KIAA0933;
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), TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND VARIANTS GLY-1118 AND HIS-1149.
RX PubMed=10950924; DOI=10.1006/geno.2000.6250;
RA Guipponi M., Brunschwig K., Chamoun Z., Scott H.S., Shibuya K., Kudoh J.,
RA Delezoide A.-L., El Samadi S., Chettouh Z., Rossier C., Shimizu N.,
RA Mueller F., Delabar J.-M., Antonarakis S.E.;
RT "C21orf5, a novel human chromosome 21 gene, has a Caenorhabditis elegans
RT ortholog (pad-1) required for embryonic patterning.";
RL Genomics 68:30-40(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Shibuya K., Kudoh J., Minoshima S., Kawasaki K., Nakatoh E., Shintani A.,
RA Asakawa S., Shimizu N.;
RT "Genomic sequencing of 1.2-Mb region on human chromosome 21q22.2.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
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] OF 152-2298 (ISOFORM 1), AND VARIANT
RP GLU-2139.
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [6]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1428-2298 (ISOFORM 2).
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 [8]
RP IDENTIFICATION.
RX PubMed=10931277; DOI=10.1046/j.1365-2958.2000.01950.x;
RA Pascon R.C., Miller B.L.;
RT "Morphogenesis in Aspergillus nidulans requires Dopey (DopA), a member of a
RT novel family of leucine zipper-like proteins conserved from yeast to
RT humans.";
RL Mol. Microbiol. 36:1250-1264(2000).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=12767918; DOI=10.1016/s0006-291x(03)00867-2;
RA Lopes C., Chettouh Z., Delabar J.-M., Rachidi M.;
RT "The differentially expressed C21orf5 gene in the medial temporal-lobe
RT system could play a role in mental retardation in Down syndrome and
RT transgenic mice.";
RL Biochem. Biophys. Res. Commun. 305:915-924(2003).
RN [10]
RP DEVELOPMENTAL STAGE.
RX PubMed=16276086; DOI=10.1159/000087509;
RA Rachidi M., Lopes C., Delezoide A.-L., Delabar J.-M.;
RT "C21orf5, a human candidate gene for brain abnormalities and mental
RT retardation in Down syndrome.";
RL Cytogenet. Genome Res. 112:16-22(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [13]
RP FUNCTION, INTERACTION WITH SNX3; ATP9A AND MON2, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=30213940; DOI=10.1038/s41467-018-06114-3;
RA McGough I.J., de Groot R.E.A., Jellett A.P., Betist M.C., Varandas K.C.,
RA Danson C.M., Heesom K.J., Korswagen H.C., Cullen P.J.;
RT "SNX3-retromer requires an evolutionary conserved MON2:DOPEY2:ATP9A complex
RT to mediate Wntless sorting and Wnt secretion.";
RL Nat. Commun. 9:3737-3737(2018).
CC -!- FUNCTION: May play a role in regulating membrane trafficking of cargo
CC proteins. Together with ATP9A and MON2, regulates SNX3 retromer-
CC mediated endosomal sorting of WLS away from lysosomal degradation.
CC {ECO:0000269|PubMed:30213940}.
CC -!- SUBUNIT: Homooligomer (PubMed:30213940). Heterotrimer with ATP9A and
CC MON2; this interaction is retromer-independent (PubMed:30213940).
CC Interacts with SNX3 (PubMed:30213940). {ECO:0000269|PubMed:30213940}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000269|PubMed:30213940}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q03921}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q03921}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y3R5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y3R5-2; Sequence=VSP_027387;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Overexpressed in
CC lymphoblasts from Down syndrome patients. {ECO:0000269|PubMed:10950924,
CC ECO:0000269|PubMed:12767918}.
CC -!- DEVELOPMENTAL STAGE: Abundantly expressed in developing central nervous
CC system, with highest levels in cerebellum and lowest in telencephalon.
CC {ECO:0000269|PubMed:10950924, ECO:0000269|PubMed:16276086}.
CC -!- SIMILARITY: Belongs to the dopey family. {ECO:0000305}.
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DR EMBL; AJ237839; CAB41415.1; -; mRNA.
DR EMBL; AP000692; BAA89431.1; -; Genomic_DNA.
DR EMBL; AP000689; BAA89431.1; JOINED; Genomic_DNA.
DR EMBL; AP000690; BAA89431.1; JOINED; Genomic_DNA.
DR EMBL; AP000691; BAA89431.1; JOINED; Genomic_DNA.
DR EMBL; AP001725; BAA95548.1; -; Genomic_DNA.
DR EMBL; AB023150; BAA76777.2; -; mRNA.
DR EMBL; CH471079; EAX09743.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09744.1; -; Genomic_DNA.
DR EMBL; BC012791; AAH12791.1; -; mRNA.
DR CCDS; CCDS13643.1; -. [Q9Y3R5-1]
DR RefSeq; NP_001307643.1; NM_001320714.1. [Q9Y3R5-1]
DR RefSeq; NP_005119.2; NM_005128.3. [Q9Y3R5-1]
DR AlphaFoldDB; Q9Y3R5; -.
DR BioGRID; 115302; 51.
DR IntAct; Q9Y3R5; 6.
DR MINT; Q9Y3R5; -.
DR STRING; 9606.ENSP00000382104; -.
DR GlyGen; Q9Y3R5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y3R5; -.
DR PhosphoSitePlus; Q9Y3R5; -.
DR BioMuta; DOPEY2; -.
DR DMDM; 311033496; -.
DR EPD; Q9Y3R5; -.
DR jPOST; Q9Y3R5; -.
DR MassIVE; Q9Y3R5; -.
DR MaxQB; Q9Y3R5; -.
DR PaxDb; Q9Y3R5; -.
DR PeptideAtlas; Q9Y3R5; -.
DR PRIDE; Q9Y3R5; -.
DR ProteomicsDB; 86069; -. [Q9Y3R5-1]
DR ProteomicsDB; 86070; -. [Q9Y3R5-2]
DR Antibodypedia; 54117; 22 antibodies from 9 providers.
DR DNASU; 9980; -.
DR Ensembl; ENST00000399151.3; ENSP00000382104.3; ENSG00000142197.13. [Q9Y3R5-1]
DR Ensembl; ENST00000691173.1; ENSP00000509598.1; ENSG00000142197.13. [Q9Y3R5-1]
DR GeneID; 9980; -.
DR KEGG; hsa:9980; -.
DR MANE-Select; ENST00000691173.1; ENSP00000509598.1; NM_001320714.2; NP_001307643.1.
DR UCSC; uc002yvg.4; human. [Q9Y3R5-1]
DR CTD; 9980; -.
DR DisGeNET; 9980; -.
DR GeneCards; DOP1B; -.
DR HGNC; HGNC:1291; DOP1B.
DR HPA; ENSG00000142197; Low tissue specificity.
DR MIM; 604803; gene.
DR neXtProt; NX_Q9Y3R5; -.
DR OpenTargets; ENSG00000142197; -.
DR PharmGKB; PA25845; -.
DR VEuPathDB; HostDB:ENSG00000142197; -.
DR eggNOG; KOG3613; Eukaryota.
DR GeneTree; ENSGT00390000016421; -.
DR HOGENOM; CLU_001045_0_0_1; -.
DR InParanoid; Q9Y3R5; -.
DR OMA; NHSAYNT; -.
DR OrthoDB; 29961at2759; -.
DR PhylomeDB; Q9Y3R5; -.
DR TreeFam; TF316855; -.
DR PathwayCommons; Q9Y3R5; -.
DR SignaLink; Q9Y3R5; -.
DR BioGRID-ORCS; 9980; 10 hits in 1071 CRISPR screens.
DR ChiTaRS; DOPEY2; human.
DR GeneWiki; DOPEY2; -.
DR GenomeRNAi; 9980; -.
DR Pharos; Q9Y3R5; Tbio.
DR PRO; PR:Q9Y3R5; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; Q9Y3R5; protein.
DR Bgee; ENSG00000142197; Expressed in cortical plate and 145 other tissues.
DR ExpressionAtlas; Q9Y3R5; baseline and differential.
DR Genevisible; Q9Y3R5; HS.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:HGNC-UCL.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0050890; P:cognition; IMP:UniProtKB.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISS:HGNC-UCL.
DR GO; GO:0006895; P:Golgi to endosome transport; ISS:HGNC-UCL.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR040314; DOP1.
DR InterPro; IPR007249; Dopey_N.
DR PANTHER; PTHR14042; PTHR14042; 1.
DR Pfam; PF04118; Dopey_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endosome; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..2298
FT /note="Protein dopey-2"
FT /id="PRO_0000190974"
FT REGION 577..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHQ6"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHQ6"
FT MOD_RES 1169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHQ6"
FT VAR_SEQ 1871..1877
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027387"
FT VARIANT 1021
FT /note="S -> W (in dbSNP:rs7278340)"
FT /id="VAR_034688"
FT VARIANT 1118
FT /note="C -> G (in dbSNP:rs4817788)"
FT /evidence="ECO:0000269|PubMed:10950924"
FT /id="VAR_027939"
FT VARIANT 1149
FT /note="P -> H (in dbSNP:rs3746866)"
FT /evidence="ECO:0000269|PubMed:10950924"
FT /id="VAR_027940"
FT VARIANT 1217
FT /note="R -> S (in dbSNP:rs3746867)"
FT /id="VAR_027941"
FT VARIANT 2139
FT /note="G -> E (in dbSNP:rs3827183)"
FT /evidence="ECO:0000269|PubMed:10231032"
FT /id="VAR_027942"
FT CONFLICT 498
FT /note="Q -> H (in Ref. 1; CAB41415)"
FT /evidence="ECO:0000305"
FT CONFLICT 1318
FT /note="L -> P (in Ref. 1; CAB41415)"
FT /evidence="ECO:0000305"
FT CONFLICT 1886
FT /note="V -> A (in Ref. 1; CAB41415)"
FT /evidence="ECO:0000305"
FT CONFLICT 1974
FT /note="E -> G (in Ref. 1; CAB41415)"
FT /evidence="ECO:0000305"
FT CONFLICT 2154
FT /note="K -> R (in Ref. 1; CAB41415)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2298 AA; 258230 MW; ED317E61F297B8C3 CRC64;
MDPEEQELLN DYRYRSYSSV IEKALRNFES SSEWADLISS LGKLNKALQS NLRYSLLPRR
LLISKRLAQC LHPALPSGVH LKALETYEII FKIVGTKWLA KDLFLYSCGL FPLLAHAAVS
VRPVLLTLYE KYFLPLQKLL LPSLQAFIVG LLPGLEEGSE ISDRTDALLL RLSLVVGKEV
FYTALWGSVL ASPSIRLPAS VFVVGHINRD APGREQKYML GTNHQLTVKS LRASLLDSNV
LVQRNNLEIV LFFFPFYTCL DSNERAIPLL RSDIVRILSA ATQTLLRRDM SLNRRLYAWL
LGSDIKGNTV VPESEISNSY EDQSSYFFEK YSKDLLVEGL AEILHQKFID ADVEERHHAY
LKPFRVLISL LDKPEIGPQV VGNLFLEVIR AFYSYCRDAL GSDLKLSYTQ SGNSLISAIK
ENRNASEIVK TVNLLITSLS TDFLWDYMTR CFEECFRPVK QRYSVRNSVS PPPTVSELCA
LLVFLLDVIP LELYSEVQTQ YLPQVLGCLV QPLAEDMEAL SLPELTHALK TCFKVLSKVQ
MPPSYLDTES TSGTSSPVKG ENGKIILETK AVIPGDEDAS FPPLKSEDSG IGLSASSPEL
SEHLRVPRVS LERDDVWKKG GSMQRTFLCI QELIANFASK NIFGVQLTAS GEESKSEEPA
GKRDRDGTQS LAANDSSRKN SWEPKPITVP QFKQMLSDLF TARGSPFKTK SSESPSSSPS
SPARKNGGEW DVEKVVIDLG GSREERREAF AAACHLLLDC ATFPVYLSEE ETEQLCATLF
QLPGAGDSSF PSWLKSLMTI CCCVTDCYLQ NVAISTLLEV INHSQSLALV IEDKMKRYKS
SGHNPFFGKL QMVTVPPIAP GILKVIAEKT DFYQRVARVL WNQLNKETRE HHVTCVELFY
RLHCLAPTAN ICEDIICHAL LDPDKGTRLE ALFRFSVIWH LTREIQGSRV TSHNRSFDRS
LFVVLDSLAC TDGAIGAAAQ GWLVRALSLG DVARILEPVL LLLLQPKTQR TSIHCLKQEN
SADDLHRWFN RKKTSFREAC AVPEPQESGS EEHLPLSQFT TVDREAIWAE VEKEPEKYPL
RGELSEEELP YYVELPDRTA HGAPDSSEHT ESADTSSCHT DSENTSSFSS PSHDLQELSN
EENCCAPIPM GGRAYPKRSA LLAAFQSESF KAGAKLSLVR VDSDKTQASE SFSSDEEADL
ELQALTTSRL LKQQRERQEA VEALFKHILL YLQPYDSRRV LYAFSVLEAV LKTNPKEFIE
AVSRTSMDTS STAHLNLISN LLARHQEALI GQSFYGKLQT QVPNVCPHSL LLELLTYLCL
SFLRSYYPCY LKVSHRDILG NRDVQVKSVE VLIRIMMQLV SVAKSSEGKN VEFIHSLLQR
CKVQEFVLLS LSASMYTSQK RYGLATAHHG RALPEDSLFE ESLINLGQDQ IWSEHPLQIE
LLKLLQVLIV LEHHLGRAHE EAENQPDLSR EWQRALNFQQ AISALQYVQP HPLTSQGLLV
SAVVRGLQPA YGYGMHPAWV SLVTHSLPYF GKSLGWTVTP FVVQICKNLD DLVKQYESES
VKLSVSTTSK RENISPDYPL TLLEGLTTIS HFCLLEQANQ NKKTMAAGDP ANLRNARNAI
LEELPRTVNT MALLWNVLRK EETQKRPVDL LGATKGSSSV YFKTTKTIRQ KILDFLNPLT
AHLGVQLTAA VAAVWSRKKA QRHSKMKIIP TASASQLTLV DLVCALSTLQ TDTLLHLVKE
VVKRPPQVKG GDEKSPLVDI PVLQFCYAFL QRLPVPALQE NFSSLLGVLK ESVQLNLAPP
GYFLLLSMLN DFVTRTPNLE NKKDQKDLQE ITQKILEAVG NIAGSSLEQT SWLSRNLEVK
AQPQASLEES DAEEDLYDAA AASAMVSSSA PSVYSVQALS LLAEVLASLL DMVYRSDEKE
KAVPLISRLL YYVFPYLRNH SAYNAPSFRA GAQLLSSLSG YAYTKRAWRK EVLELFLDPA
FFQMDTSCVH WKSIIDHLLT HEKTMFKDLM NMQSSSLKLF SSFEQKAMLL KRQAFAVFSG
ELDQYHLYLP LIQERLTDNL RVGQTSIVAA QMFLFFRVLL LRISPQHLTS LWPIMVSELI
QTFTQLEEDL KDEDESLRST NKVNRTKVSV PDANGPSVGE IPQSELILYL SACKFLDTAL
SFPPDKMPLF QIYRWAFIPE VDTEGPAFLS DVEENHQECK PHTVRILELL KLKFGEISSS
DEITMKSEFP LLRQHSVSSI RQLMPFFMTL NGAFKTQRQL PADSPGTPFL DFPVTDSPRI
LKQLEECIEY DFLEHPEC
