ARVC_HUMAN
ID ARVC_HUMAN Reviewed; 962 AA.
AC O00192; B7WNV2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Splicing regulator ARVCF {ECO:0000305};
DE AltName: Full=Armadillo repeat protein deleted in velo-cardio-facial syndrome {ECO:0000305};
GN Name=ARVCF {ECO:0000312|HGNC:HGNC:728};
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 LONG AND SHORT).
RX PubMed=9126485; DOI=10.1006/geno.1997.4627;
RA Sirotkin H., O'Donnell H., DasGupta R., Halford S., St Jore B., Puech A.,
RA Parimoo S., Morrow B., Skoultchi A., Weissman S., Scambler P.,
RA Kucherlapati R.;
RT "Identification of a new human catenin gene family member (ARVCF) from the
RT region deleted in velo-cardio-facial syndrome.";
RL Genomics 41:75-83(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10725230; DOI=10.1242/jcs.113.8.1481;
RA Mariner D.J., Wang J., Reynolds A.B.;
RT "ARVCF localizes to the nucleus and adherens junction and is mutually
RT exclusive with p120(ctn) in E-cadherin complexes.";
RL J. Cell Sci. 113:1481-1490(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-864, 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 [5]
RP INTERACTION WITH FRMPD2.
RX PubMed=19706687; DOI=10.1242/jcs.046854;
RA Stenzel N., Fetzer C.P., Heumann R., Erdmann K.S.;
RT "PDZ-domain-directed basolateral targeting of the peripheral membrane
RT protein FRMPD2 in epithelial cells.";
RL J. Cell Sci. 122:3374-3384(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-871 AND THR-872, VARIANT
RP [LARGE SCALE ANALYSIS] GLN-906, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-864, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-642; SER-864 AND SER-915, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [9]
RP FUNCTION, IDENTIFICATION IN RIBONUCLEOPROTEIN COMPLEX, INTERACTION WITH
RP DDX5; HNRNPH2 AND SRSF1, AND SUBCELLULAR LOCATION.
RX PubMed=24644279; DOI=10.1074/jbc.m113.530717;
RA Rappe U., Schlechter T., Aschoff M., Hotz-Wagenblatt A., Hofmann I.;
RT "Nuclear ARVCF protein binds splicing factors and contributes to the
RT regulation of alternative splicing.";
RL J. Biol. Chem. 289:12421-12434(2014).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-102; THR-104; SER-267;
RP SER-332; SER-335; SER-343; SER-345; SER-606 AND THR-642, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP INTERACTION WITH CCDC85B.
RX PubMed=25009281; DOI=10.1091/mbc.e13-08-0492;
RA Markham N.O., Doll C.A., Dohn M.R., Miller R.K., Yu H., Coffey R.J.,
RA McCrea P.D., Gamse J.T., Reynolds A.B.;
RT "DIPA-family coiled-coils bind conserved isoform-specific head domain of
RT p120-catenin family: potential roles in hydrocephalus and heterotopia.";
RL Mol. Biol. Cell 25:2592-2603(2014).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=29034528; DOI=10.1111/ced.13214;
RA Abreu-Velez A.M., Valencia-Yepes C.A., Upegui-Zapata Y.A.,
RA Upegui-Quiceno E., Mesa-Herrera N.R., Velazquez-Velez J.E., Howard M.S.;
RT "Patients with a new variant of endemic pemphigus foliaceus have
RT autoantibodies against arrector pili muscle, colocalizing with MYZAP,
RT p0071, desmoplakins 1 and 2 and ARVCF.";
RL Clin. Exp. Dermatol. 42:874-880(2017).
RN [13]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=30479852; DOI=10.5826/dpc.0804a02;
RA Abreu-Velez A.M., Howard M.S., Padilla H.J.L., Tobon-Arroyave S.;
RT "Subclinical oral involvement in patients with endemic pemphigus
RT foliaceus.";
RL Dermatol. Pract. Concept. 8:252-261(2018).
CC -!- FUNCTION: Contributes to the regulation of alternative splicing of pre-
CC mRNAs. {ECO:0000269|PubMed:24644279}.
CC -!- SUBUNIT: Component of a ribonucleoprotein complex containing mRNAs and
CC RNA-binding proteins including DDX5, HNRNPH2 and SRSF1 as well as ARVCF
CC (PubMed:24644279). Interacts (via the extreme C-terminus) with FRMPD2
CC (via the PDZ 2 domain) (PubMed:19706687). Interacts with CCDC85B
CC (PubMed:25009281). {ECO:0000269|PubMed:19706687,
CC ECO:0000269|PubMed:24644279, ECO:0000269|PubMed:25009281}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000269|PubMed:10725230, ECO:0000269|PubMed:24644279,
CC ECO:0000305|PubMed:30479852}. Nucleus {ECO:0000269|PubMed:10725230,
CC ECO:0000269|PubMed:24644279}. Cytoplasm {ECO:0000269|PubMed:24644279}.
CC Note=In heart, localizes at area composita, the mixed-type junctional
CC structure composed of both desmosomal and adherens junctional proteins.
CC {ECO:0000250|UniProtKB:B4F7F3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=O00192-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=O00192-2; Sequence=VSP_006739;
CC -!- TISSUE SPECIFICITY: Found in all the examined tissues including heart,
CC brain, liver and kidney. Found at low level in lung. Expressed in
CC dermal connective tissue, salivary gland duct and in the corneal layer
CC (at protein level) (PubMed:30479852). Expressed in arrector pili muscle
CC (at protein level) (PubMed:29034528). High levels detected in
CC epithelial cells with lower levels found in fibroblasts and T
CC lymphocytes (PubMed:10725230). {ECO:0000269|PubMed:10725230,
CC ECO:0000269|PubMed:29034528, ECO:0000269|PubMed:30479852}.
CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
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DR EMBL; U51269; AAC51202.1; -; mRNA.
DR EMBL; AC005663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS13771.1; -. [O00192-1]
DR RefSeq; NP_001661.1; NM_001670.2. [O00192-1]
DR RefSeq; XP_006724310.1; XM_006724247.3. [O00192-2]
DR RefSeq; XP_011528482.1; XM_011530180.1. [O00192-1]
DR AlphaFoldDB; O00192; -.
DR SMR; O00192; -.
DR BioGRID; 106914; 53.
DR IntAct; O00192; 14.
DR MINT; O00192; -.
DR STRING; 9606.ENSP00000263207; -.
DR iPTMnet; O00192; -.
DR PhosphoSitePlus; O00192; -.
DR SwissPalm; O00192; -.
DR BioMuta; ARVCF; -.
DR EPD; O00192; -.
DR jPOST; O00192; -.
DR MassIVE; O00192; -.
DR MaxQB; O00192; -.
DR PaxDb; O00192; -.
DR PeptideAtlas; O00192; -.
DR PRIDE; O00192; -.
DR ProteomicsDB; 47770; -. [O00192-1]
DR ProteomicsDB; 47771; -. [O00192-2]
DR Antibodypedia; 4255; 92 antibodies from 23 providers.
DR DNASU; 421; -.
DR Ensembl; ENST00000263207.8; ENSP00000263207.3; ENSG00000099889.14. [O00192-1]
DR Ensembl; ENST00000401994.5; ENSP00000384341.1; ENSG00000099889.14. [O00192-2]
DR GeneID; 421; -.
DR KEGG; hsa:421; -.
DR MANE-Select; ENST00000263207.8; ENSP00000263207.3; NM_001670.3; NP_001661.1.
DR UCSC; uc002zqz.4; human. [O00192-1]
DR CTD; 421; -.
DR DisGeNET; 421; -.
DR GeneCards; ARVCF; -.
DR HGNC; HGNC:728; ARVCF.
DR HPA; ENSG00000099889; Low tissue specificity.
DR MalaCards; ARVCF; -.
DR MIM; 602269; gene.
DR neXtProt; NX_O00192; -.
DR OpenTargets; ENSG00000099889; -.
DR Orphanet; 567; 22q11.2 deletion syndrome.
DR PharmGKB; PA25018; -.
DR VEuPathDB; HostDB:ENSG00000099889; -.
DR eggNOG; KOG1048; Eukaryota.
DR GeneTree; ENSGT00940000157027; -.
DR HOGENOM; CLU_009111_1_0_1; -.
DR InParanoid; O00192; -.
DR OMA; CGQPLPM; -.
DR OrthoDB; 233858at2759; -.
DR PhylomeDB; O00192; -.
DR TreeFam; TF321877; -.
DR PathwayCommons; O00192; -.
DR SignaLink; O00192; -.
DR SIGNOR; O00192; -.
DR BioGRID-ORCS; 421; 18 hits in 1083 CRISPR screens.
DR ChiTaRS; ARVCF; human.
DR GeneWiki; ARVCF; -.
DR GenomeRNAi; 421; -.
DR Pharos; O00192; Tbio.
DR PRO; PR:O00192; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O00192; protein.
DR Bgee; ENSG00000099889; Expressed in cerebellar hemisphere and 189 other tissues.
DR ExpressionAtlas; O00192; baseline and differential.
DR Genevisible; O00192; HS.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; IPI:UniProtKB.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR028444; ARVCF.
DR InterPro; IPR028435; Plakophilin/d_Catenin.
DR PANTHER; PTHR10372; PTHR10372; 1.
DR PANTHER; PTHR10372:SF5; PTHR10372:SF5; 1.
DR Pfam; PF00514; Arm; 4.
DR SMART; SM00185; ARM; 6.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell junction; Coiled coil; Cytoplasm;
KW Methylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..962
FT /note="Splicing regulator ARVCF"
FT /id="PRO_0000064294"
FT REPEAT 348..387
FT /note="ARM 1"
FT REPEAT 390..429
FT /note="ARM 2"
FT REPEAT 433..467
FT /note="ARM 3"
FT REPEAT 468..508
FT /note="ARM 4"
FT REPEAT 526..565
FT /note="ARM 5"
FT REPEAT 575..622
FT /note="ARM 6"
FT REPEAT 646..686
FT /note="ARM 7"
FT REPEAT 699..738
FT /note="ARM 8"
FT REPEAT 739..781
FT /note="ARM 9"
FT REPEAT 782..826
FT /note="ARM 10"
FT REGION 95..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..962
FT /note="Required for interaction with RNA-binding proteins
FT DDX5, HNRNPH2 and SRSF1 and with mRNAs"
FT /evidence="ECO:0000269|PubMed:24644279"
FT REGION 854..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 8..46
FT /evidence="ECO:0000255"
FT MOTIF 607..623
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 98..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 102
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 170
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P98203"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 642
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 864
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 871
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 872
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..69
FT /note="MEDCNVHSAASILASVKEQEARFERLTRALEQERRHVALQLERAQQPGMVSG
FT GMGSGQPLPMAWQQLVL -> MPAELR (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:9126485"
FT /id="VSP_006739"
FT VARIANT 175
FT /note="V -> A (in dbSNP:rs2240717)"
FT /id="VAR_020408"
FT VARIANT 220
FT /note="P -> L (in dbSNP:rs2073748)"
FT /id="VAR_033529"
FT VARIANT 539
FT /note="R -> Q (in dbSNP:rs16982871)"
FT /id="VAR_053812"
FT VARIANT 906
FT /note="R -> Q (in dbSNP:rs165815)"
FT /evidence="ECO:0007744|PubMed:19690332"
FT /id="VAR_024692"
FT VARIANT 909
FT /note="R -> Q (in dbSNP:rs34638476)"
FT /id="VAR_033531"
FT VARIANT 909
FT /note="R -> W (in dbSNP:rs34687532)"
FT /id="VAR_033530"
FT VARIANT 912
FT /note="R -> W (in dbSNP:rs34445280)"
FT /id="VAR_033532"
SQ SEQUENCE 962 AA; 104642 MW; 74A1814A022FF2B1 CRC64;
MEDCNVHSAA SILASVKEQE ARFERLTRAL EQERRHVALQ LERAQQPGMV SGGMGSGQPL
PMAWQQLVLQ EQSPGSQASL ATMPEAPDVL EETVTVEEDP GTPTSHVSIV TSEDGTTRRT
ETKVTKTVKT VTTRTVRQVP VGPDGLPLLD GGPPLGPFAD GALDRHFLLR GGGPVATLSR
AYLSSGGGFP EGPEPRDSPS YGSLSRGLGM RPPRAGPLGP GPGDGCFTLP GHREAFPVGP
EPGPPGGRSL PERFQAEPYG LEDDTRSLAA DDEGGPELEP DYGTATRRRP ECGRGLHTRA
YEDTADDGGE LADERPAFPM VTAPLAQPER GSMGSLDRLV RRSPSVDSAR KEPRWRDPEL
PEVLAMLRHP VDPVKANAAA YLQHLCFENE GVKRRVRQLR GLPLLVALLD HPRAEVRRRA
CGALRNLSYG RDTDNKAAIR DCGGVPALVR LLRAARDNEV RELVTGTLWN LSSYEPLKMV
IIDHGLQTLT HEVIVPHSGW EREPNEDSKP RDAEWTTVFK NTSGCLRNVS SDGAEARRRL
RECEGLVDAL LHALQSAVGR KDTDNKSVEN CVCIMRNLSY HVHKEVPGAD RYQEAEPGPL
GSAVGSQRRR RDDASCFGGK KAKEEWFHQG KKDGEMDRNF DTLDLPKRTE AAKGFELLYQ
PEVVRLYLSL LTESRNFNTL EAAAGALQNL SAGNWMWATY IRATVRKERG LPVLVELLQS
ETDKVVRAVA IALRNLSLDR RNKDLIGSYA MAELVRNVRN AQAPPRPGAC LEEDTVVAVL
NTIHEIVSDS LDNARSLLQA RGVPALVALV ASSQSVREAK AASHVLQTVW SYKELRGTLQ
KDGWTKARFQ SAAATAKGPK GALSPGGFDD STLPLVDKSL EGEKTGSRDV IPMDALGPDG
YSTVDRRERR PRGASSAGEA SEKEPLKLDP SRKAPPPGPS RPAVRLVDAV GDAKPQPVDS
WV
