ZFY26_MOUSE
ID ZFY26_MOUSE Reviewed; 2529 AA.
AC Q5DU37; B9EJ71; Q3TEM9; Q3V1N3; Q8BY74; Q8CDR8; Q923B4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Zinc finger FYVE domain-containing protein 26;
GN Name=Zfyve26; Synonyms=Kiaa0321;
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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 2027-2529 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head, Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic intestine;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, and 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1732; SER-1770 AND SER-1772,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC 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).
CC -!- FUNCTION: Phosphatidylinositol 3-phosphate-binding protein required for
CC the abcission step in cytokinesis: recruited to the midbody during
CC cytokinesis and acts as a regulator of abcission. May also be required
CC for efficient homologous recombination DNA double-strand break repair
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with AP5Z1, AP5B1, AP5S1 and SPG11. Interacts with
CC TTC19 and KIF13A (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Midbody {ECO:0000250}. Note=Localizes
CC to the centrosome during all stages of the cell cycle. Recruited to the
CC midbody during cytokinesis by KIF13A (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5DU37-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5DU37-2; Sequence=VSP_030343;
CC Name=3;
CC IsoId=Q5DU37-3; Sequence=VSP_030342, VSP_030344, VSP_030345,
CC VSP_030346;
CC -!- DOMAIN: The FYVE-type zinc finger mediates binding to
CC phosphatidylinositol 3-phosphate and recruitment to the midbody during
CC cytokinesis. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ZFYVE26 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90401.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK029679; BAC26561.1; -; mRNA.
DR EMBL; AK041668; BAC31027.1; -; mRNA.
DR EMBL; AK132344; BAE21117.1; -; mRNA.
DR EMBL; AK169541; BAE41219.1; -; mRNA.
DR EMBL; AK220333; BAD90401.1; ALT_INIT; mRNA.
DR EMBL; BC006654; AAH06654.1; -; mRNA.
DR EMBL; BC141359; AAI41360.1; -; mRNA.
DR CCDS; CCDS36481.1; -. [Q5DU37-1]
DR RefSeq; NP_001008550.1; NM_001008550.1. [Q5DU37-1]
DR AlphaFoldDB; Q5DU37; -.
DR BioGRID; 229279; 2.
DR IntAct; Q5DU37; 2.
DR STRING; 10090.ENSMUSP00000021547; -.
DR iPTMnet; Q5DU37; -.
DR PhosphoSitePlus; Q5DU37; -.
DR EPD; Q5DU37; -.
DR MaxQB; Q5DU37; -.
DR PaxDb; Q5DU37; -.
DR PeptideAtlas; Q5DU37; -.
DR PRIDE; Q5DU37; -.
DR ProteomicsDB; 299554; -. [Q5DU37-1]
DR ProteomicsDB; 299555; -. [Q5DU37-2]
DR ProteomicsDB; 299556; -. [Q5DU37-3]
DR Antibodypedia; 24903; 82 antibodies from 26 providers.
DR Ensembl; ENSMUST00000021547; ENSMUSP00000021547; ENSMUSG00000066440. [Q5DU37-1]
DR GeneID; 211978; -.
DR KEGG; mmu:211978; -.
DR UCSC; uc007oae.1; mouse. [Q5DU37-1]
DR UCSC; uc007oaf.1; mouse. [Q5DU37-3]
DR UCSC; uc007oah.1; mouse. [Q5DU37-2]
DR CTD; 23503; -.
DR MGI; MGI:1924767; Zfyve26.
DR VEuPathDB; HostDB:ENSMUSG00000066440; -.
DR eggNOG; KOG1811; Eukaryota.
DR GeneTree; ENSGT00920000149143; -.
DR HOGENOM; CLU_228199_0_0_1; -.
DR InParanoid; Q5DU37; -.
DR OMA; RAYLTCC; -.
DR OrthoDB; 1237900at2759; -.
DR PhylomeDB; Q5DU37; -.
DR TreeFam; TF324517; -.
DR BioGRID-ORCS; 211978; 3 hits in 108 CRISPR screens.
DR ChiTaRS; Zfyve26; mouse.
DR PRO; PR:Q5DU37; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q5DU37; protein.
DR Bgee; ENSMUSG00000066440; Expressed in granulocyte and 242 other tissues.
DR ExpressionAtlas; Q5DU37; baseline and differential.
DR Genevisible; Q5DU37; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:1905037; P:autophagosome organization; ISO:MGI.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0007040; P:lysosome organization; ISO:MGI.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:InterPro.
DR GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR028730; ZFYVE26.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46591; PTHR46591; 1.
DR Pfam; PF01363; FYVE; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; DNA damage; DNA repair; Lipid-binding; Metal-binding;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..2529
FT /note="Zinc finger FYVE domain-containing protein 26"
FT /id="PRO_0000314613"
FT ZN_FING 1802..1862
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 584..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1258..1286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1762..1799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1865..1884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 859..884
FT /evidence="ECO:0000255"
FT COILED 1488..1515
FT /evidence="ECO:0000255"
FT COMPBIAS 689..703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..766
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1865..1880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1808
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1811
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1825
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1828
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1833
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1836
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1854
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1857
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A8G9"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68DK2"
FT MOD_RES 791
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68DK2"
FT MOD_RES 1732
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1754
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68DK2"
FT MOD_RES 1770
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1772
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..1714
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030342"
FT VAR_SEQ 1201..2529
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030343"
FT VAR_SEQ 1715..1730
FT /note="AGKALDLPYPLREKRS -> MLVVEQCFVSSLSLSA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030344"
FT VAR_SEQ 2368..2370
FT /note="MLG -> RRL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030345"
FT VAR_SEQ 2371..2529
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030346"
FT CONFLICT 495
FT /note="M -> V (in Ref. 1; BAE21117)"
FT /evidence="ECO:0000305"
FT CONFLICT 1180
FT /note="Q -> H (in Ref. 3; AAI41360)"
FT /evidence="ECO:0000305"
FT CONFLICT 2489
FT /note="A -> V (in Ref. 3; AAH06654)"
FT /evidence="ECO:0000305"
FT CONFLICT 2525
FT /note="S -> C (in Ref. 3; AAH06654)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2529 AA; 282961 MW; 1885B6B0421066FD CRC64;
MSYPFGKEET ATEEELFEFF CECLRRGDWE LAQACVPQLH RGQGEIPQKV EDILQALVQC
PILLRCGPDI NPQRLAWLWL LVLEKWLAPE KKLLSTAIRR KLEFLFLSED LQGDIPETIL
KELFETLAQG PAGSIPDRRT PQLSPEAVSV LWNLLKQAPR PAQALLELLL EDHHSASLCP
SPLQKSLLDL IREALQTLRD PASQPPGVAD AVCGALQALC CKAELPESEW RVLCEELLET
CRTEDSPLQE ERLLGCLLHK AGRNLLSLYG HTYAEKVAER PPKATLSGKD HPDPERAMLA
LFSTPDPAHA WKMAFFYCLS NNKHFLEQIL VTALTLLKEE DFPSLGYLLD REFRPLSHLL
VLLGWTHCQS LESAKRLLQT LYRTQDQGHD ELLRDACEGL WAHLEVLEWC VQQSSNLIPK
RELLCHLHGG DSHSVLYSLH HLTNLPALNE EEVLKLLQKE PTKDLQGEHE THDASVPEHL
SQCQSLTLYQ GFCAMKYAVY ALCVNSHQHS QCQDCRDSAS EDLALVEPGS DSLPSPGASH
LFPTYLARCR QYLHSIPASL CLEILENIFS LLLITSADLH PEPHLPEDYA EDEDIEGKGP
LGLRSPSESP QHIAATERRS ERASMGPRNP AHTVPGCPKA EPKDSSPGPH KHSFLDLKHF
TSGVNGFLAD EFAMGAFLSL LQEQLTEISS HRTPEETKLP EDQSCSAARD GLQSRLHRFS
KVLSEAQWRY KVVTSNQGSE EQPSRRYRPI ATRHSSLRRG RRTRRTRADG RERGSNPSLE
GTSSELSTST SEGSLSAVSG QVESDSRFQT QPQSSIIPMM FSTPESLLAS CILRGNFAEA
HQVVLMFNLK SSPIAGELMF VERYQEVIQE LARVEHKIEN QNSDGGNNTI RRTGSGRSTL
QAIGSAAAAG MVFYSISDVT EKLLSPSEDP IPTLQEDFWI NATPMETTTP LREVLEDLSP
PAMAAFDLAC CQCQLWKTCK QLLETAERRL SSSLESRGRR LDQVVLNPDG MRGFPFVLQQ
ISKILSYPLM QTGLAKSETL EERGGGAPRS SISELLQMCW PSLTEDCVAS HTSLSQQLEQ
ALQSLREALA LPESKSTPLS CLVEQAAQKA PEAEAHPVHI QSQLLQKTLG RQTPAGHRQT
DYVGAFFSYC SSLAAVLLRS LSSDPDHVEV RVGNPFVLLQ QSSSQLVSHL LLERQVPPDR
LAALLAQEHL NLSVPQVIVS CCCEPLTLCL SRQSQQASSL LTHLGMLARE HASHLLDGLP
LSTLGSPRPS ENPSAERKSH SSPKDSLPAF TASALAFLKS RSKILAMVAC LRTSRGTKVS
KPGLSWKELR GRREAPLTAE KVAQECEHLL EQFPVFEAAL LANWEPLQQA SEPKQSLAAS
LCGQANLSTV LLGLHSSLAL DILTEAFEGA LVARDWPRAL QLIDVYGQDL DDLSIVQDSV
LTCAAVCDKE GWQYLFPVKD ASLRSQLALR FVDKWPLESC LEILAYCVSD MAVQEELKSE
LQRKLMELRV YQKILGLQDP PVWCDWQTLR SCCAEDPSAV MDMMLDSQEY ELCEEWGRLY
PIPREHLVSL HHKHLLHLLE RSEHDKALQL LQRIPDPTMC LEVTERSLDQ HPSLATSHFL
ANYLTSHFYG ELTTDRHREI QALYMGSKVL LTLPEQHRAS YARLSSSPLL MLEQLLMNMK
VDWATTAVQT LHQLLAGQDI GFTLDEVDSL LSRYAGKALD LPYPLREKRS DSMIHLQEPV
HQASDSETLS RSSSAEFSAA AAPGSALVRS PSPKERAFPQ TQPPVEFVPP ETPPARDQWV
PDETESVCMV CCREHFTMFN RRHHCRRCGR LVCGSCSTKK MVVEGFRENP TRVCDQCYSY
YNKDTPEESP CQSEVPDSAK NESPPYSAVV RVPKATEVEW ILSLSEEENE LVRSEFYYEQ
APSASLCIAI LNLHRDSIAC GHQLIEHCCR LSRGLTNPEV DAGLLIDIMK QLLFSAKMMF
VKAGQSQDLA LCDSYISKVD VLHLLVAAAY RHVPSLDQIL QPAAVTRLRN QLLEAEYYQL
GVEVSTKTGL DSTGAWHAWG MACLKAGNLT VAREKFTRCL KPPLDLNQLS HGSRLVQDVV
EYLESTVRPL VSLQDDDYFA TLRELEATLR TQSLLLEAIP EGKIMNNTYY QECLFYLHNY
STNLAIISFY MRHNCLREAL LHLLNKESPP EVFIEGIFQP SYKSGKLHTL ENLLESIDPT
LESWGAHLIA ACQHLQKNSY YHILYELQQF MKDQVRAAMT CIRFFSHKAK SYTELGEKLS
WLLKAKDHLK IYLQETSRSS GRKKATFFRK KMTAADVSRH MNTLQLQMEV TRFLHRCESA
GTSQVTTLPL PTLFGNNHMK MEVACKVMLG GKNVEDGFGI AFRVLQDFQL DAAATYCRAA
RQLVEREKYG EIRQLLKCVS ESGMAAKSDG DTILLNCLEA FKRIPPQELE GLIQAIHSDD
NKVRAYLTCC KLRSAYLIAV KQEHSQAAAL VQQVQQAAKS SGDSVVQDIC AQWLLTSHSR
GAHGSGSRK
