CASD1_HUMAN
ID CASD1_HUMAN Reviewed; 797 AA.
AC Q96PB1; B3KW13; O14574; Q3LIE2; Q6P4R4; Q9H6T9; Q9H770;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=N-acetylneuraminate 9-O-acetyltransferase {ECO:0000305};
DE EC=2.3.1.45 {ECO:0000269|PubMed:26169044};
DE AltName: Full=CAS1 domain-containing protein 1 {ECO:0000305};
DE AltName: Full=Sialate O-acetyltransferase {ECO:0000303|PubMed:20947662, ECO:0000303|PubMed:26169044};
DE Short=SOAT {ECO:0000303|PubMed:20947662, ECO:0000303|PubMed:26169044};
GN Name=CASD1 {ECO:0000312|HGNC:HGNC:16014}; Synonyms=C7orf12;
GN ORFNames=Nbla04196;
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].
RC TISSUE=Brain;
RA Grabowski M., Zimprich A., Strom T.M.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-386.
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 335-797.
RC TISSUE=Neuroblastoma;
RX PubMed=12880961; DOI=10.1016/s0304-3835(03)00085-5;
RA Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S.,
RA Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S.,
RA Hirato J., Nakagawara A.;
RT "Neuroblastoma oligo-capping cDNA project: toward the understanding of the
RT genesis and biology of neuroblastoma.";
RL Cancer Lett. 197:63-68(2003).
RN [7]
RP FUNCTION.
RX PubMed=20947662; DOI=10.1093/glycob/cwq153;
RA Arming S., Wipfler D., Mayr J., Merling A., Vilas U., Schauer R.,
RA Schwartz-Albiez R., Vlasak R.;
RT "The human Cas1 protein: a sialic acid-specific O-acetyltransferase?";
RL Glycobiology 21:553-564(2011).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=21507905; DOI=10.1093/glycob/cwr050;
RA Wipfler D., Srinivasan G.V., Sadick H., Kniep B., Arming S.,
RA Willhauck-Fleckenstein M., Vlasak R., Schauer R., Schwartz-Albiez R.;
RT "Differentially regulated expression of 9-O-acetyl GD3 (CD60b) and 7-O-
RT acetyl-GD3 (CD60c) during differentiation and maturation of human T and B
RT lymphocytes.";
RL Glycobiology 21:1161-1172(2011).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, SUBCELLULAR LOCATION,
RP GLYCOSYLATION, TOPOLOGY, AND MUTAGENESIS OF SER-94.
RX PubMed=26169044; DOI=10.1038/ncomms8673;
RA Baumann A.M., Bakkers M.J., Buettner F.F., Hartmann M., Grove M.,
RA Langereis M.A., de Groot R.J., Muehlenhoff M.;
RT "9-O-Acetylation of sialic acids is catalysed by CASD1 via a covalent
RT acetyl-enzyme intermediate.";
RL Nat. Commun. 6:7673-7673(2015).
CC -!- FUNCTION: O-acetyltransferase that catalyzes 9-O-acetylation of sialic
CC acids (PubMed:20947662, PubMed:26169044). Sialic acids are sugars at
CC the reducing end of glycoproteins and glycolipids, and are involved in
CC various processes such as cell-cell interactions, host-pathogen
CC recognition (PubMed:20947662, PubMed:26169044).
CC {ECO:0000269|PubMed:26169044, ECO:0000305|PubMed:20947662}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-acetylneuraminate = CoA + N-acetyl-9-O-
CC acetylneuraminate; Xref=Rhea:RHEA:26043, ChEBI:CHEBI:28999,
CC ChEBI:CHEBI:35418, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.45;
CC Evidence={ECO:0000269|PubMed:26169044};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-acetylneuraminate = CoA + N-acetyl-7-O-
CC acetylneuraminate; Xref=Rhea:RHEA:20808, ChEBI:CHEBI:28944,
CC ChEBI:CHEBI:35418, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.45;
CC Evidence={ECO:0000269|PubMed:26169044};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:26169044}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in peripheral B lymphocytes.
CC {ECO:0000269|PubMed:21507905}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:26169044}.
CC -!- SIMILARITY: Belongs to the PC-esterase family. CASD1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB69978.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB15028.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB15163.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15163.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF397424; AAK97479.2; -; mRNA.
DR EMBL; AK024866; BAB15028.1; ALT_FRAME; mRNA.
DR EMBL; AK025532; BAB15163.1; ALT_SEQ; mRNA.
DR EMBL; AK123866; BAG53975.1; -; mRNA.
DR EMBL; AC002528; AAB69978.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC096662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236949; EAL24136.1; -; Genomic_DNA.
DR EMBL; BC063284; AAH63284.1; -; mRNA.
DR EMBL; AB073397; BAE45726.1; -; mRNA.
DR CCDS; CCDS5636.1; -.
DR RefSeq; NP_075051.4; NM_022900.4.
DR AlphaFoldDB; Q96PB1; -.
DR SMR; Q96PB1; -.
DR BioGRID; 122344; 9.
DR STRING; 9606.ENSP00000297273; -.
DR GlyConnect; 1077; 1 N-Linked glycan (1 site).
DR GlyGen; Q96PB1; 5 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q96PB1; -.
DR PhosphoSitePlus; Q96PB1; -.
DR BioMuta; CASD1; -.
DR DMDM; 74717082; -.
DR EPD; Q96PB1; -.
DR jPOST; Q96PB1; -.
DR MassIVE; Q96PB1; -.
DR MaxQB; Q96PB1; -.
DR PaxDb; Q96PB1; -.
DR PeptideAtlas; Q96PB1; -.
DR PRIDE; Q96PB1; -.
DR ProteomicsDB; 77651; -.
DR Antibodypedia; 45361; 113 antibodies from 15 providers.
DR DNASU; 64921; -.
DR Ensembl; ENST00000297273.9; ENSP00000297273.4; ENSG00000127995.17.
DR GeneID; 64921; -.
DR KEGG; hsa:64921; -.
DR MANE-Select; ENST00000297273.9; ENSP00000297273.4; NM_022900.5; NP_075051.4.
DR UCSC; uc003uni.5; human.
DR CTD; 64921; -.
DR DisGeNET; 64921; -.
DR GeneCards; CASD1; -.
DR HGNC; HGNC:16014; CASD1.
DR HPA; ENSG00000127995; Low tissue specificity.
DR MalaCards; CASD1; -.
DR MIM; 611686; gene.
DR neXtProt; NX_Q96PB1; -.
DR OpenTargets; ENSG00000127995; -.
DR PharmGKB; PA143485408; -.
DR VEuPathDB; HostDB:ENSG00000127995; -.
DR eggNOG; KOG1699; Eukaryota.
DR GeneTree; ENSGT00390000004037; -.
DR HOGENOM; CLU_008003_1_0_1; -.
DR InParanoid; Q96PB1; -.
DR OMA; MIYAACF; -.
DR OrthoDB; 120492at2759; -.
DR PhylomeDB; Q96PB1; -.
DR TreeFam; TF324898; -.
DR BRENDA; 2.3.1.45; 2681.
DR PathwayCommons; Q96PB1; -.
DR BioGRID-ORCS; 64921; 7 hits in 1075 CRISPR screens.
DR ChiTaRS; CASD1; human.
DR GenomeRNAi; 64921; -.
DR Pharos; Q96PB1; Tbio.
DR PRO; PR:Q96PB1; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q96PB1; protein.
DR Bgee; ENSG00000127995; Expressed in adrenal tissue and 192 other tissues.
DR ExpressionAtlas; Q96PB1; baseline and differential.
DR Genevisible; Q96PB1; HS.
DR GO; GO:0030173; C:integral component of Golgi membrane; IDA:UniProtKB.
DR GO; GO:0047186; F:N-acetylneuraminate 7-O(or 9-O)-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR InterPro; IPR012419; Cas1_AcylTrans_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR Pfam; PF07779; Cas1_AcylT; 1.
DR SUPFAM; SSF47954; SSF47954; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..797
FT /note="N-acetylneuraminate 9-O-acetyltransferase"
FT /id="PRO_0000307230"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..313
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:26169044"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385..395
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 417..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..486
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..513
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 514..534
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 535..547
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..605
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 627..638
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 639..659
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 660..671
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 672..692
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 693..698
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 699..719
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 720..725
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 726..746
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 747..770
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 771..791
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 792..797
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT ACT_SITE 94
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000269|PubMed:26169044"
FT ACT_SITE 270
FT /evidence="ECO:0000305|PubMed:26169044"
FT ACT_SITE 273
FT /evidence="ECO:0000305|PubMed:26169044"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 386
FT /note="R -> S (in dbSNP:rs17855797)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035383"
FT MUTAGEN 94
FT /note="S->A: Abolishes O-acetyltransferase activity."
FT /evidence="ECO:0000269|PubMed:26169044"
FT CONFLICT 622
FT /note="K -> E (in Ref. 2; BAB15028)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 797 AA; 91680 MW; 28EA7CA7A1DE223C CRC64;
MAALAYNLGK REINHYFSVR SAKVLALVAV LLLAACHLAS RRYRGNDSCE YLLSSGRFLG
EKVWQPHSCM MHKYKISEAK NCLVDKHIAF IGDSRIRQLF YSFVKIINPQ FKEEGNKHEN
IPFEDKTASV KVDFLWHPEV NGSMKQCIKV WTEDSIAKPH VIVAGAATWS IKIHNGSSEA
LSQYKMNITS IAPLLEKLAK TSDVYWVLQD PVYEDLLSEN RKMITNEKID AYNEAAVSIL
NSSTRNSKSN VKMFSVSKLI AQETIMESLD GLHLPESSRE TTAMILMNVY CNKILKPVDG
SCCQPRPPVT LIQKLAACFF TLSIIGYLIF YIIHRNAHRK NKPCTDLESG EEKKNIINTP
VSSLEILLQS FCKLGLIMAY FYMCDRANLF MKENKFYTHS SFFIPIIYIL VLGVFYNENT
KETKVLNREQ TDEWKGWMQL VILIYHISGA STFLPVYMHI RVLVAAYLFQ TGYGHFSYFW
IKGDFGIYRV CQVLFRLNFL VVVLCIVMDR PYQFYYFVPL VTVWFMVIYV TLALWPQIIQ
KKANGNCFWH FGLLLKLGFL LLFICFLAYS QGAFEKIFSL WPLSKCFELK GNVYEWWFRW
RLDRYVVFHG MLFAFIYLAL QKRQILSEGK GEPLFSNKIS NFLLFISVVS FLTYSIWASS
CKNKAECNEL HPSVSVVQIL AFILIRNIPG YARSVYSSFF AWFGKISLEL FICQYHIWLA
ADTRGILVLI PGNPMLNIIV STFIFVCVAH EISQITNDLA QIIIPKDNSS LLKRLACIAA
FFCGLLILSS IQDKSKH
