ID CTNL1_HUMAN Reviewed; 734 AA. AC Q9UBT7; B5BU47; O76084; Q53FQ2; Q5JTQ7; Q5JTQ8; Q9Y401; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 2. DT 07-APR-2021, entry version 149. DE RecName: Full=Alpha-catulin; DE AltName: Full=Alpha-catenin-related protein; DE Short=ACRP; DE AltName: Full=Catenin alpha-like protein 1; GN Name=CTNNAL1; 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, AND INDUCTION. RC TISSUE=Pancreatic cancer; RX PubMed=9806841; DOI=10.1006/geno.1998.5458; RA Zhang J.-S., Nelson M., Wang L., Liu W., Qian C.-P., Shridhar V., RA Urrutia R., Smith D.I.; RT "Identification and chromosomal localization of CTNNAL1, a novel protein RT homologous to alpha-catenin."; RL Genomics 54:149-154(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND TISSUE RP SPECIFICITY. RX PubMed=10542337; DOI=10.1016/s0167-4781(99)00170-0; RA Janssens B., Staes K., van Roy F.M.; RT "Human alpha-catulin, a novel alpha-catenin-like molecule with conserved RT genomic structure, but deviating alternative splicing."; RL Biochim. Biophys. Acta 1447:341-347(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Kishi M., Nagafuchi A., Tsukita S.; RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Slaugenhaupt S.A., Liebert C.B., Leyne M., Mull J., Gill S., Chadwick B.P., RA Maayan C., Axelrod F.B., Blumenfeld A., Gusella J.F.; RT "Isolation of a novel alpha-catenin-like gene from the familial RT dysautonomia candidate region on 9q31."; RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Gastric mucosa; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-91; LYS-203; GLN-527; RP ASN-593 AND ARG-716. RG NIEHS SNPs program; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., RA Nomura N.; RT "Human protein factory for converting the transcriptome into an in vitro- RT expressed proteome."; RL Nat. Methods 5:1011-1017(2008). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [9] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 296-734 (ISOFORM 3). RC TISSUE=Brain; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [12] RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH ARHGEF1. RX PubMed=12270917; DOI=10.1074/jbc.m202447200; RA Park B., Nguyen N.T., Dutt P., Merdek K.D., Bashar M., Sterpetti P., RA Tosolini A., Testa J.R., Toksoz D.; RT "Association of Lbc Rho guanine nucleotide exchange factor with alpha- RT catenin-related protein, alpha-catulin/CTNNAL1, supports serum response RT factor activation."; RL J. Biol. Chem. 277:45361-45370(2002). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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 modulate the Rho pathway signaling by providing a CC scaffold for the Lbc Rho guanine nucleotide exchange factor (ARHGEF1). CC -!- SUBUNIT: Interacts with ARHGEF1. {ECO:0000269|PubMed:12270917}. CC -!- INTERACTION: CC Q9UBT7; Q0VDD7: BRME1; NbExp=3; IntAct=EBI-514206, EBI-741210; CC Q9UBT7; Q8NA61: CBY2; NbExp=3; IntAct=EBI-514206, EBI-741724; CC Q9UBT7; P11532: DMD; NbExp=8; IntAct=EBI-514206, EBI-295827; CC Q9UBT7; Q9Y4J8: DTNA; NbExp=5; IntAct=EBI-514206, EBI-949471; CC Q9UBT7; O60941: DTNB; NbExp=2; IntAct=EBI-514206, EBI-740402; CC Q9UBT7; Q00722: PLCB2; NbExp=3; IntAct=EBI-514206, EBI-968381; CC Q9UBT7; Q8IUD6: RNF135; NbExp=6; IntAct=EBI-514206, EBI-9916363; CC Q9UBT7; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-514206, EBI-748621; CC Q9UBT7; Q9C029: TRIM7; NbExp=3; IntAct=EBI-514206, EBI-2813981; CC Q9UBT7; Q9Y3Q8: TSC22D4; NbExp=3; IntAct=EBI-514206, EBI-739485; CC Q9UBT7; Q9Y6N9: USH1C; NbExp=3; IntAct=EBI-514206, EBI-954308; CC Q9UBT7; O96006: ZBED1; NbExp=3; IntAct=EBI-514206, EBI-740037; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:12270917}. Cell membrane CC {ECO:0000269|PubMed:12270917}; Peripheral membrane protein CC {ECO:0000269|PubMed:12270917}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9UBT7-1; Sequence=Displayed; CC Name=2; Synonyms=Alpha2-catulin; CC IsoId=Q9UBT7-2; Sequence=VSP_012583; CC Name=3; CC IsoId=Q9UBT7-3; Sequence=VSP_012582; CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at lower level in CC neural tissues and at the highest level in the adrenal gland. CC {ECO:0000269|PubMed:10542337, ECO:0000269|PubMed:12270917, CC ECO:0000269|PubMed:9806841}. CC -!- INDUCTION: Down-regulated in cancer pancreatic cells undergoing CC differentiation and apoptosis. {ECO:0000269|PubMed:9806841}. CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/ctnnal1/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF030233; AAC83460.1; -; mRNA. DR EMBL; U97067; AAC27693.1; -; mRNA. DR EMBL; AF134888; AAF07820.1; -; Genomic_DNA. DR EMBL; AF134871; AAF07820.1; JOINED; Genomic_DNA. DR EMBL; AF134873; AAF07820.1; JOINED; Genomic_DNA. DR EMBL; AF134874; AAF07820.1; JOINED; Genomic_DNA. DR EMBL; AF134872; AAF07820.1; JOINED; Genomic_DNA. DR EMBL; AF134875; AAF07820.1; JOINED; Genomic_DNA. DR EMBL; AF134877; AAF07820.1; JOINED; Genomic_DNA. DR EMBL; AF134879; AAF07820.1; JOINED; Genomic_DNA. DR EMBL; AF134881; AAF07820.1; JOINED; Genomic_DNA. DR EMBL; AF134887; AAF07820.1; JOINED; Genomic_DNA. DR EMBL; AF134886; AAF07820.1; JOINED; Genomic_DNA. DR EMBL; AF134885; AAF07820.1; JOINED; Genomic_DNA. DR EMBL; AF134884; AAF07820.1; JOINED; Genomic_DNA. DR EMBL; AF134883; AAF07820.1; JOINED; Genomic_DNA. DR EMBL; AF134882; AAF07820.1; JOINED; Genomic_DNA. DR EMBL; AF134880; AAF07820.1; JOINED; Genomic_DNA. DR EMBL; AF134878; AAF07820.1; JOINED; Genomic_DNA. DR EMBL; AF134876; AAF07820.1; JOINED; Genomic_DNA. DR EMBL; AF134888; AAF07821.1; -; Genomic_DNA. DR EMBL; AF134871; AAF07821.1; JOINED; Genomic_DNA. DR EMBL; AF134872; AAF07821.1; JOINED; Genomic_DNA. DR EMBL; AF134874; AAF07821.1; JOINED; Genomic_DNA. DR EMBL; AF134876; AAF07821.1; JOINED; Genomic_DNA. DR EMBL; AF134878; AAF07821.1; JOINED; Genomic_DNA. DR EMBL; AF134880; AAF07821.1; JOINED; Genomic_DNA. DR EMBL; AF134882; AAF07821.1; JOINED; Genomic_DNA. DR EMBL; AF134884; AAF07821.1; JOINED; Genomic_DNA. DR EMBL; AF134887; AAF07821.1; JOINED; Genomic_DNA. DR EMBL; AF134886; AAF07821.1; JOINED; Genomic_DNA. DR EMBL; AF134885; AAF07821.1; JOINED; Genomic_DNA. DR EMBL; AF134883; AAF07821.1; JOINED; Genomic_DNA. DR EMBL; AF134881; AAF07821.1; JOINED; Genomic_DNA. DR EMBL; AF134879; AAF07821.1; JOINED; Genomic_DNA. DR EMBL; AF134877; AAF07821.1; JOINED; Genomic_DNA. DR EMBL; AF134875; AAF07821.1; JOINED; Genomic_DNA. DR EMBL; AF134873; AAF07821.1; JOINED; Genomic_DNA. DR EMBL; AF135021; AAF07819.1; -; mRNA. DR EMBL; AF006070; AAC26011.1; -; mRNA. DR EMBL; AF080071; AAC69576.1; -; mRNA. DR EMBL; AK223230; BAD96950.1; -; mRNA. DR EMBL; AY523969; AAR92479.1; -; Genomic_DNA. DR EMBL; AB451283; BAG70097.1; -; mRNA. DR EMBL; AB451415; BAG70229.1; -; mRNA. DR EMBL; AL354797; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471105; EAW59036.1; -; Genomic_DNA. DR EMBL; BC117208; AAI17209.1; -; mRNA. DR EMBL; BC117234; AAI17235.1; -; mRNA. DR EMBL; AL050016; CAB43238.1; -; mRNA. DR CCDS; CCDS6775.1; -. [Q9UBT7-1] DR CCDS; CCDS69638.1; -. [Q9UBT7-2] DR PIR; T08703; T08703. DR RefSeq; NP_001273903.1; NM_001286974.1. [Q9UBT7-2] DR RefSeq; NP_003789.1; NM_003798.3. [Q9UBT7-1] DR SMR; Q9UBT7; -. DR BioGRID; 114266; 30. DR CORUM; Q9UBT7; -. DR DIP; DIP-33236N; -. DR IntAct; Q9UBT7; 33. DR MINT; Q9UBT7; -. DR STRING; 9606.ENSP00000320434; -. DR iPTMnet; Q9UBT7; -. DR PhosphoSitePlus; Q9UBT7; -. DR BioMuta; CTNNAL1; -. DR DMDM; 62901512; -. DR EPD; Q9UBT7; -. DR jPOST; Q9UBT7; -. DR MassIVE; Q9UBT7; -. DR PaxDb; Q9UBT7; -. DR PeptideAtlas; Q9UBT7; -. DR PRIDE; Q9UBT7; -. DR ProteomicsDB; 84061; -. [Q9UBT7-1] DR ProteomicsDB; 84062; -. [Q9UBT7-2] DR ProteomicsDB; 84063; -. [Q9UBT7-3] DR Antibodypedia; 14981; 142 antibodies. DR DNASU; 8727; -. DR Ensembl; ENST00000325551; ENSP00000320434; ENSG00000119326. [Q9UBT7-1] DR Ensembl; ENST00000374595; ENSP00000363723; ENSG00000119326. [Q9UBT7-2] DR GeneID; 8727; -. DR KEGG; hsa:8727; -. DR UCSC; uc004bdo.3; human. [Q9UBT7-1] DR CTD; 8727; -. DR DisGeNET; 8727; -. DR GeneCards; CTNNAL1; -. DR HGNC; HGNC:2512; CTNNAL1. DR HPA; ENSG00000119326; Tissue enhanced (adrenal). DR MIM; 604785; gene. DR neXtProt; NX_Q9UBT7; -. DR OpenTargets; ENSG00000119326; -. DR PharmGKB; PA27011; -. DR VEuPathDB; HostDB:ENSG00000119326.14; -. DR eggNOG; KOG3681; Eukaryota. DR GeneTree; ENSGT00990000203614; -. DR HOGENOM; CLU_015314_4_0_1; -. DR InParanoid; Q9UBT7; -. DR OMA; NEIVQHG; -. DR PhylomeDB; Q9UBT7; -. DR TreeFam; TF313686; -. DR PathwayCommons; Q9UBT7; -. DR BioGRID-ORCS; 8727; 8 hits in 998 CRISPR screens. DR ChiTaRS; CTNNAL1; human. DR GeneWiki; CTNNAL1; -. DR GenomeRNAi; 8727; -. DR Pharos; Q9UBT7; Tbio. DR PRO; PR:Q9UBT7; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q9UBT7; protein. DR Bgee; ENSG00000119326; Expressed in right adrenal gland cortex and 237 other tissues. DR ExpressionAtlas; Q9UBT7; baseline and differential. DR Genevisible; Q9UBT7; HS. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051015; F:actin filament binding; IEA:InterPro. DR GO; GO:0045296; F:cadherin binding; IEA:InterPro. DR GO; GO:0007155; P:cell adhesion; IEA:InterPro. DR GO; GO:0007266; P:Rho protein signal transduction; IDA:MGI. DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf. DR InterPro; IPR001033; Alpha_catenin. DR InterPro; IPR030045; CTNNAL1. DR InterPro; IPR006077; Vinculin/catenin. DR PANTHER; PTHR46342; PTHR46342; 1. DR Pfam; PF01044; Vinculin; 1. DR PRINTS; PR00805; ALPHACATENIN. DR SUPFAM; SSF47220; SSF47220; 3. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Cytoplasm; Cytoskeleton; Membrane; KW Phosphoprotein; Reference proteome. FT CHAIN 1..734 FT /note="Alpha-catulin" FT /id="PRO_0000064268" FT MOD_RES 374 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O88327" FT MOD_RES 538 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 397..480 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_012582" FT VAR_SEQ 714..734 FT /note="LQMENNGWVSVTNKDTMDSKT -> SETRY (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10542337" FT /id="VSP_012583" FT VARIANT 91 FT /note="N -> T (in dbSNP:rs28361109)" FT /evidence="ECO:0000269|Ref.6" FT /id="VAR_020924" FT VARIANT 203 FT /note="E -> K (in dbSNP:rs28361118)" FT /evidence="ECO:0000269|Ref.6" FT /id="VAR_020925" FT VARIANT 424 FT /note="T -> S (in dbSNP:rs16913734)" FT /id="VAR_033845" FT VARIANT 527 FT /note="E -> Q (in dbSNP:rs7021366)" FT /evidence="ECO:0000269|Ref.6" FT /id="VAR_020926" FT VARIANT 555 FT /note="D -> E (in dbSNP:rs34922868)" FT /id="VAR_053370" FT VARIANT 593 FT /note="I -> N (in dbSNP:rs28361167)" FT /evidence="ECO:0000269|Ref.6" FT /id="VAR_020927" FT VARIANT 716 FT /note="M -> R (in dbSNP:rs28361182)" FT /evidence="ECO:0000269|Ref.6" FT /id="VAR_020928" FT CONFLICT 504 FT /note="F -> S (in Ref. 5; BAD96950)" FT /evidence="ECO:0000305" SQ SEQUENCE 734 AA; 81896 MW; 8756237C73AAEA31 CRC64; MAASPGPAGV GGAGAVYGSG SSGFALDSGL EIKTRSVEQT LLPLVSQITT LINHKDNTKK SDKTLQAIQR VGQAVNLAVG RFVKVGEAIA NENWDLKEEI NIACIEAKQA GETIAALTDI TNLNHLESDG QITIFTDKTG VIKAARLLLS SVTKVLLLAD RVVIKQIITS RNKVLATMER LEKVNSFQEF VQIFSQFGNE MVEFAHLSGD RQNDLKDEKK KAKMAAARAV LEKCTMMLLT ASKTCLRHPN CESAHKNKEG VFDRMKVALD KVIEIVTDCK PNGETDISSI SIFTGIKEFK MNIEALRENL YFQSKENLSV TLEVILERME DFTDSAYTSH EHRERILELS TQARMELQQL ISVWIQAQSK KTKSIAEELE LSILKISHSL NELKKELHST ATQLAADLLK YHADHVVLKA LKLTGVEGNL EALAEYACKL SEQKEQLVET CRLLRHISGT EPLEITCIHA EETFQVTGQQ IISAAETLTL HPSSKIAKEN LDVFCEAWES QISDMSTLLR EINDVFEGRR GEKYGYLSLP KPMKNNANLK SLKPDKPDSE EQAKIAKLGL KLGLLTSDAD CEIEKWEDQE NEIVQYGRNM SSMAYSLYLF TRGEGPLKTS QDLIHQLEVF AAEGLKLTSS VQAFSKQLKD DDKLMLLLEI NKLIPLCHQL QTVTKTSLQN KVFLKVDKCI TKTRSMMALL VQLLSLCYKL LKKLQMENNG WVSVTNKDTM DSKT //