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   27-MAR-2024, entry version 159.
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; 31.
DR   CORUM; Q8IWY9; -.
DR   DIP; DIP-24225N; -.
DR   IntAct; Q8IWY9; 6.
DR   MINT; Q8IWY9; -.
DR   STRING; 9606.ENSP00000348564; -.
DR   GlyGen; Q8IWY9; 1 site, 1 O-linked glycan (1 site).
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; 9606-ENSP00000348564; -.
DR   PeptideAtlas; Q8IWY9; -.
DR   ProteomicsDB; 70932; -. [Q8IWY9-2]
DR   ProteomicsDB; 70933; -. [Q8IWY9-1]
DR   Pumba; Q8IWY9; -.
DR   ABCD; Q8IWY9; 1 sequenced antibody.
DR   Antibodypedia; 42152; 150 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   AGR; HGNC:1713; -.
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; 2909919at2759; -.
DR   PhylomeDB; Q8IWY9; -.
DR   TreeFam; TF328405; -.
DR   PathwayCommons; Q8IWY9; -.
DR   SignaLink; Q8IWY9; -.
DR   BioGRID-ORCS; 146059; 490 hits in 1178 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 158 other cell types or tissues.
DR   ExpressionAtlas; Q8IWY9; baseline and differential.
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:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0006325; P:chromatin organization; IMP:MGI.
DR   GO; GO:0051170; P:import into nucleus; IMP:GO_Central.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   InterPro; IPR040031; Codanin-1.
DR   InterPro; IPR028171; Codanin-1_C.
DR   PANTHER; PTHR28678; CODANIN-1; 1.
DR   PANTHER; PTHR28678:SF1; CODANIN-1; 1.
DR   Pfam; PF15296; Codanin-1_C; 1.
DR   Genevisible; Q8IWY9; HS.
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
//