CTNL1_HUMAN
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 03-AUG-2022, entry version 154.
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/";
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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 AlphaFoldDB; Q9UBT7; -.
DR SMR; Q9UBT7; -.
DR BioGRID; 114266; 54.
DR CORUM; Q9UBT7; -.
DR DIP; DIP-33236N; -.
DR IntAct; Q9UBT7; 37.
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 MaxQB; 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; 144 antibodies from 27 providers.
DR DNASU; 8727; -.
DR Ensembl; ENST00000325551.9; ENSP00000320434.4; ENSG00000119326.15. [Q9UBT7-1]
DR Ensembl; ENST00000374595.8; ENSP00000363723.4; ENSG00000119326.15. [Q9UBT7-2]
DR GeneID; 8727; -.
DR KEGG; hsa:8727; -.
DR MANE-Select; ENST00000325551.9; ENSP00000320434.4; NM_003798.4; NP_003789.1.
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; -.
DR eggNOG; KOG3681; Eukaryota.
DR GeneTree; ENSGT01030000234543; -.
DR HOGENOM; CLU_015314_4_0_1; -.
DR InParanoid; Q9UBT7; -.
DR OMA; DQQKMAK; -.
DR PhylomeDB; Q9UBT7; -.
DR TreeFam; TF313686; -.
DR PathwayCommons; Q9UBT7; -.
DR SignaLink; Q9UBT7; -.
DR BioGRID-ORCS; 8727; 12 hits in 1087 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 206 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
