CDAN1_HUMAN
ID CDAN1_HUMAN Reviewed; 1227 AA.
AC Q8IWY9; Q6NYD0; Q7Z7L5; Q969N3;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 4.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Codanin-1;
GN Name=CDAN1; ORFNames=UNQ664/PRO1295;
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 3), TISSUE SPECIFICITY, AND
RP VARIANTS CDAN1A SER-599; LEU-672; LYS-698; TRP-714; ILE-868; MET-869;
RP TRP-1042; VAL-1043 AND LEU-1130.
RX PubMed=12434312; DOI=10.1086/344781;
RA Dgany O., Avidan N., Delaunay J., Krasnov T., Shalmon L., Shalev H.,
RA Eidelitz-Markus T., Kapelushnik J., Cattan D., Pariente A., Tulliez M.,
RA Cretien A., Schischmanoff P.-O., Iolascon A., Fibach E., Koren A.,
RA Roessler J., Le Merrer M., Yaniv I., Zaizov R., Ben-Asher E., Olender T.,
RA Lancet D., Beckmann J.S., Tamary H.;
RT "Congenital dyserythropoietic anemia type I is caused by mutations in
RT codanin-1.";
RL Am. J. Hum. Genet. 71:1467-1474(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney, and Ovary;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 669-1016 (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=21364188; DOI=10.1182/blood-2010-09-308478;
RA Renella R., Roberts N.A., Brown J.M., De Gobbi M., Bird L.E., Hassanali T.,
RA Sharpe J.A., Sloane-Stanley J., Ferguson D.J., Cordell J., Buckle V.J.,
RA Higgs D.R., Wood W.G.;
RT "Codanin-1 mutations in congenital dyserythropoietic anemia type 1 affect
RT HP1-alpha localization in erythroblasts.";
RL Blood 117:6928-6938(2011).
RN [6]
RP SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH ASF1A AND ASF1B,
RP IDENTIFICATION IN A COMPLEX WITH ASF1A; ASF1B; IPO4; HISTONES H3.2 AND H4,
RP CHARACTERIZATION OF VARIANTS TRP-714 AND TRP-1042, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=22407294; DOI=10.1038/emboj.2012.55;
RA Ask K., Jasencakova Z., Menard P., Feng Y., Almouzni G., Groth A.;
RT "Codanin-1, mutated in the anaemic disease CDAI, regulates Asf1 function in
RT S-phase histone supply.";
RL EMBO J. 31:2013-2023(2012).
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=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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-71; SER-265 AND SER-285, 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).
CC -!- FUNCTION: May act as a negative regulator of ASF1 in chromatin
CC assembly. {ECO:0000269|PubMed:22407294}.
CC -!- SUBUNIT: Found in a cytosolic complex with ASF1A, ASF1B, IPO4 and
CC histones H3.1 and H4. {ECO:0000269|PubMed:22407294}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}. Note=Mainly detected as a
CC cytoplasmic protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=2;
CC IsoId=Q8IWY9-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q8IWY9-1; Sequence=VSP_027097, VSP_027098;
CC Name=3;
CC IsoId=Q8IWY9-3; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 3 is not found in
CC erythroid cells. {ECO:0000269|PubMed:12434312}.
CC -!- DISEASE: Anemia, congenital dyserythropoietic, 1A (CDAN1A)
CC [MIM:224120]: An autosomal recessive blood disorder characterized by
CC morphological abnormalities of erythroblasts, ineffective
CC erythropoiesis, macrocytic anemia and secondary hemochromatosis. It is
CC occasionally associated with bone abnormalities, especially of the
CC hands and feet (acrodysostosis), nail hypoplasia, and scoliosis.
CC Ultrastructural features include internuclear chromatin bridges
CC connecting some nearly completely separated erythroblasts and an
CC abnormal appearance (spongy or Swiss-cheese appearance) of the
CC heterochromatin in a high proportion of the erythroblasts.
CC {ECO:0000269|PubMed:12434312}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH52568.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO14994.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAQ88832.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF525398; AAO14994.1; ALT_INIT; mRNA.
DR EMBL; AC090510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001092; AAH01092.1; -; mRNA.
DR EMBL; BC008333; AAH08333.1; -; mRNA.
DR EMBL; BC008334; AAH08334.1; -; mRNA.
DR EMBL; BC052568; AAH52568.1; ALT_INIT; mRNA.
DR EMBL; BC066640; AAH66640.1; -; mRNA.
DR EMBL; AY358467; AAQ88832.1; ALT_INIT; mRNA.
DR CCDS; CCDS32209.1; -. [Q8IWY9-2]
DR RefSeq; NP_612486.2; NM_138477.2. [Q8IWY9-2]
DR AlphaFoldDB; Q8IWY9; -.
DR BioGRID; 126963; 29.
DR CORUM; Q8IWY9; -.
DR DIP; DIP-24225N; -.
DR IntAct; Q8IWY9; 6.
DR MINT; Q8IWY9; -.
DR STRING; 9606.ENSP00000348564; -.
DR iPTMnet; Q8IWY9; -.
DR PhosphoSitePlus; Q8IWY9; -.
DR BioMuta; CDAN1; -.
DR DMDM; 296439465; -.
DR EPD; Q8IWY9; -.
DR jPOST; Q8IWY9; -.
DR MassIVE; Q8IWY9; -.
DR MaxQB; Q8IWY9; -.
DR PaxDb; Q8IWY9; -.
DR PeptideAtlas; Q8IWY9; -.
DR PRIDE; Q8IWY9; -.
DR ProteomicsDB; 70932; -. [Q8IWY9-2]
DR ProteomicsDB; 70933; -. [Q8IWY9-1]
DR ABCD; Q8IWY9; 1 sequenced antibody.
DR Antibodypedia; 42152; 136 antibodies from 20 providers.
DR DNASU; 146059; -.
DR Ensembl; ENST00000356231.4; ENSP00000348564.3; ENSG00000140326.13. [Q8IWY9-2]
DR GeneID; 146059; -.
DR KEGG; hsa:146059; -.
DR MANE-Select; ENST00000356231.4; ENSP00000348564.3; NM_138477.4; NP_612486.2.
DR UCSC; uc001zql.4; human. [Q8IWY9-2]
DR CTD; 146059; -.
DR DisGeNET; 146059; -.
DR GeneCards; CDAN1; -.
DR GeneReviews; CDAN1; -.
DR HGNC; HGNC:1713; CDAN1.
DR HPA; ENSG00000140326; Low tissue specificity.
DR MalaCards; CDAN1; -.
DR MIM; 224120; phenotype.
DR MIM; 607465; gene.
DR neXtProt; NX_Q8IWY9; -.
DR OpenTargets; ENSG00000140326; -.
DR Orphanet; 98869; Congenital dyserythropoietic anemia type I.
DR PharmGKB; PA26249; -.
DR VEuPathDB; HostDB:ENSG00000140326; -.
DR eggNOG; ENOG502QPWR; Eukaryota.
DR GeneTree; ENSGT00390000000491; -.
DR HOGENOM; CLU_007378_0_0_1; -.
DR InParanoid; Q8IWY9; -.
DR OMA; CVVKDAQ; -.
DR OrthoDB; 664227at2759; -.
DR PhylomeDB; Q8IWY9; -.
DR TreeFam; TF328405; -.
DR PathwayCommons; Q8IWY9; -.
DR SignaLink; Q8IWY9; -.
DR BioGRID-ORCS; 146059; 473 hits in 1091 CRISPR screens.
DR ChiTaRS; CDAN1; human.
DR GenomeRNAi; 146059; -.
DR Pharos; Q8IWY9; Tbio.
DR PRO; PR:Q8IWY9; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8IWY9; protein.
DR Bgee; ENSG00000140326; Expressed in ventricular zone and 156 other tissues.
DR ExpressionAtlas; Q8IWY9; baseline and differential.
DR Genevisible; Q8IWY9; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0012505; C:endomembrane system; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0031497; P:chromatin assembly; IMP:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IMP:MGI.
DR GO; GO:0008156; P:negative regulation of DNA replication; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR InterPro; IPR040031; Codanin-1.
DR InterPro; IPR028171; Codanin-1_C.
DR PANTHER; PTHR28678; PTHR28678; 1.
DR Pfam; PF15296; Codanin-1_C; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Congenital dyserythropoietic anemia;
KW Cytoplasm; Disease variant; Hereditary hemolytic anemia; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..1227
FT /note="Codanin-1"
FT /id="PRO_0000089439"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 626..646
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 63..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..208
FT /note="Interaction with ASF1A/B"
FT /evidence="ECO:0000269|PubMed:22407294"
FT COMPBIAS 116..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 71
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 190
FT /note="G -> GETQLSCRRWVPRRLWGVSHSSSALRSGAPGCR (in isoform
FT 1)"
FT /evidence="ECO:0000303|PubMed:12434312"
FT /id="VSP_027097"
FT VAR_SEQ 226..258
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:12434312"
FT /id="VSP_027098"
FT VARIANT 107
FT /note="Q -> L (in dbSNP:rs4265781)"
FT /id="VAR_059602"
FT VARIANT 596
FT /note="Q -> R (in dbSNP:rs12917189)"
FT /id="VAR_056785"
FT VARIANT 599
FT /note="N -> S (in CDAN1A; dbSNP:rs120074166)"
FT /evidence="ECO:0000269|PubMed:12434312"
FT /id="VAR_017218"
FT VARIANT 672
FT /note="P -> L (in CDAN1A; dbSNP:rs120074167)"
FT /evidence="ECO:0000269|PubMed:12434312"
FT /id="VAR_017219"
FT VARIANT 698
FT /note="E -> K (in CDAN1A)"
FT /evidence="ECO:0000269|PubMed:12434312"
FT /id="VAR_017220"
FT VARIANT 714
FT /note="R -> W (in CDAN1A; partially disrupts ASF1 binding
FT and loss the ability to arrest cells in S phase and inhibit
FT DNA synthesis; dbSNP:rs80338696)"
FT /evidence="ECO:0000269|PubMed:12434312,
FT ECO:0000269|PubMed:22407294"
FT /id="VAR_017221"
FT VARIANT 868
FT /note="F -> I (in CDAN1A; dbSNP:rs120074168)"
FT /evidence="ECO:0000269|PubMed:12434312"
FT /id="VAR_017222"
FT VARIANT 869
FT /note="V -> M (in CDAN1A; dbSNP:rs370895637)"
FT /evidence="ECO:0000269|PubMed:12434312"
FT /id="VAR_017223"
FT VARIANT 891
FT /note="R -> C (in dbSNP:rs8023524)"
FT /id="VAR_056786"
FT VARIANT 1042
FT /note="R -> W (in CDAN1A; partially disrupts ASF1 binding;
FT dbSNP:rs80338697)"
FT /evidence="ECO:0000269|PubMed:12434312,
FT ECO:0000269|PubMed:22407294"
FT /id="VAR_017224"
FT VARIANT 1043
FT /note="D -> V (in CDAN1A; dbSNP:rs80338698)"
FT /evidence="ECO:0000269|PubMed:12434312"
FT /id="VAR_017225"
FT VARIANT 1130
FT /note="P -> L (in CDAN1A; dbSNP:rs80338699)"
FT /evidence="ECO:0000269|PubMed:12434312"
FT /id="VAR_017226"
FT CONFLICT 31..32
FT /note="DN -> VT (in Ref. 1; AAO14994)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="L -> V (in Ref. 1; AAO14994)"
FT /evidence="ECO:0000305"
FT CONFLICT 42..45
FT /note="LRAL -> FGAW (in Ref. 1; AAO14994)"
FT /evidence="ECO:0000305"
FT CONFLICT 51..52
FT /note="PF -> RS (in Ref. 1; AAO14994)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="N -> T (in Ref. 1; AAO14994)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="A -> P (in Ref. 1; AAO14994)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="P -> R (in Ref. 1; AAO14994)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="L -> C (in Ref. 1; AAO14994)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="S -> T (in Ref. 1; AAO14994)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="V -> F (in Ref. 1; AAO14994)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="S -> F (in Ref. 3; AAH52568/AAH66640)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="Q -> P (in Ref. 4; AAQ88832)"
FT /evidence="ECO:0000305"
FT CONFLICT 726
FT /note="S -> C (in Ref. 1; AAO14994)"
FT /evidence="ECO:0000305"
FT CONFLICT 946
FT /note="R -> W (in Ref. 3; AAH01092/AAH08333/AAH08334)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1227 AA; 134120 MW; E2BC04ACD669DF6F CRC64;
MAAVLESLLR EEVSVAAVVR WIARSTQGSE DNAGEAAALS SLRALRKEFV PFLLNFLREQ
SSRVLPQGPP TPAKTPGASA ALPGRPGGPP RGSRGARSQL FPPTEAQSTA AEAPLARRGG
RRRGPGPARE RGGRGLEEGV SGESLPGAGG RRLRGSGSPS RPSLTLSDPP NLSNLEEFPP
VGSVPPGPTG TKPSRRINPT PVSEERSLSK PKTCFTSPPI SCVPSSQPSA LDTSPWGLGL
PPGCRSLQEE REMLRKERSK QLQQSPTPTC PTPELGSPLP SRTGSLTDEP ADPARVSSRQ
RLELVALVYS SCIAENLVPN LFLELFFVFQ LLTARRMVTA KDSDPELSPA VLDSLESPLF
QSIHDCVFFA VQVLECHFQV LSNLDKGTLK LLAENERLLC FSPALQGRLR AAYEGSVAKV
SLVMPPSTQA VSFQPETDNR ANFSSDRAFH TFKKQRDVFY EVLREWEDHH EEPGWDFEKG
LGSRIRAMMG QLSAACSHSH FVRLFQKQLL QMCQSPGGAG GTVLGEAPDV LSMLGADKLG
RLWRLQERLM APQSSGGPCP PPTFPGCQGF FRDFILSASS FQFNQHLMDS LSLKIQELNG
LALPQHEPND EDGESDVDWQ GERKQFAVVL LSLRLLAKFL GFVAFLPYRG PEPPPTGELQ
DSILALRSQV PPVLDVRTLL QRGLQARRAV LTVPWLVEFL SFADHVVPLL EYYRDIFTLL
LRLHRSLVLS QESEGKMCFL NKLLLLAVLG WLFQIPTVPE DLFFLEEGPS YAFEVDTVAP
EHGLDNAPVV DQQLLYTCCP YIGELRKLLA SWVSGSSGRS GGFMRKITPT TTTSLGAQPS
QTSQGLQAQL AQAFFHNQPP SLRRTVEFVA ERIGSNCVKH IKATLVADLV RQAESLLQEQ
LVTQGEEGGD PAQLLEILCS QLCPHGAQAL ALGREFCQRK SPGAVRALLP EETPAAVLSS
AENIAVGLAT EKACAWLSAN ITALIRREVK AAVSRTLRAQ GPEPAARGER RGCSRACEHH
APLPSHLISE IKDVLSLAVG PRDPDEGVSP EHLEQLLGQL GQTLRCRQFL CPPAEQHLAK
CSVELASLLV ADQIPILGPP AQYRLERGQA RRLLHMLLSL WKEDFQGPVP LQLLLSPRNV
GLLADTRPRE WDLLLFLLRE LVEKGLMGRM EIEACLGSLH QAQWPGDFAE ELATLSNLFL
AEPHLPEPQL RACELVQPNR GTVLAQS
