MYH3_HUMAN
ID MYH3_HUMAN Reviewed; 1940 AA.
AC P11055; Q15492;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Myosin-3;
DE AltName: Full=Muscle embryonic myosin heavy chain;
DE AltName: Full=Myosin heavy chain 3;
DE AltName: Full=Myosin heavy chain, fast skeletal muscle, embryonic;
DE AltName: Full=SMHCE;
GN Name=MYH3;
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], AND VARIANT THR-1192.
RX PubMed=2726495; DOI=10.1093/nar/17.9.3591;
RA Eller M.S., Stedman H.H., Sylvester J.E., Fertels S.H., Rubinstein N.A.,
RA Kelly A.M., Sarkar S.;
RT "Nucleotide sequence of full length human embryonic myosin heavy chain
RT cDNA.";
RL Nucleic Acids Res. 17:3591-3592(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 774-1940, AND VARIANT THR-1192.
RX PubMed=2806546; DOI=10.1016/0014-5793(89)81710-7;
RA Eller M.S., Stedman H.H., Sylvester J.E., Fertels S.H., Wu Q.-L.,
RA Raychowdhury M.K., Rubinstein N.A., Kelly A.M., Sarkar S.;
RT "Human embryonic myosin heavy chain cDNA. Interspecies sequence
RT conservation of the myosin rod, chromosomal locus and isoform specific
RT transcription of the gene.";
RL FEBS Lett. 256:21-28(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 856-1940, AND VARIANT THR-1192.
RC TISSUE=Skeletal muscle;
RX PubMed=1691980; DOI=10.1111/j.1432-1033.1990.tb15459.x;
RA Bober E., Buchberger-Seidl A., Braun T., Singh S., Goedde H.W.,
RA Arnold H.H.;
RT "Identification of three developmentally controlled isoforms of human
RT myosin heavy chains.";
RL Eur. J. Biochem. 189:55-65(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 856-1940, AND VARIANT THR-1192.
RX PubMed=2771643; DOI=10.1093/nar/17.15.6167;
RA Karsch-Mizrachi I., Travis M., Blau H., Leinwand L.A.;
RT "Expression and DNA sequence analysis of a human embryonic skeletal muscle
RT myosin heavy chain gene.";
RL Nucleic Acids Res. 17:6167-6179(1989).
RN [6]
RP INVOLVEMENT IN DA2A, INVOLVEMENT IN DA2B3, VARIANTS DA2A ILE-178; GLY-498;
RP SER-583; CYS-672; HIS-672 AND ASP-825, VARIANTS DA2B3 ILE-178; PHE-261;
RP CYS-292; LYS-375; TYR-517; VAL-769 AND GLU-838; LEU-841 DEL, AND VARIANTS
RP ALA-1622 AND VAL-1637.
RX PubMed=16642020; DOI=10.1038/ng1775;
RA Toydemir R.M., Rutherford A., Whitby F.G., Jorde L.B., Carey J.C.,
RA Bamshad M.J.;
RT "Mutations in embryonic myosin heavy chain (MYH3) cause Freeman-Sheldon
RT syndrome and Sheldon-Hall syndrome.";
RL Nat. Genet. 38:561-565(2006).
RN [7]
RP INVOLVEMENT IN DA2B3, VARIANT DA2A ILE-178, AND VARIANTS DA2B3 THR-234 AND
RP GLY-462.
RX PubMed=18695058; DOI=10.1001/archneur.65.8.1083;
RA Tajsharghi H., Kimber E., Kroksmark A.K., Jerre R., Tulinius M.,
RA Oldfors A.;
RT "Embryonic myosin heavy-chain mutations cause distal arthrogryposis and
RT developmental myosin myopathy that persists postnatally.";
RL Arch. Neurol. 65:1083-1090(2008).
RN [8]
RP ERRATUM OF PUBMED:18695058.
RA Tajsharghi H., Kimber E., Kroksmark A.K., Jerre R., Tulinius M.,
RA Oldfors A.;
RL Arch. Neurol. 65:1654-1654(2008).
RN [9]
RP INVOLVEMENT IN CPSFS1A, TISSUE SPECIFICITY, VARIANTS CPSFS1A SER-243 DEL;
RP ASN-1072 INS AND PRO-1075, AND CLASSIFICATION OF VARIANTS ALA-1622 AND
RP VAL-1637.
RX PubMed=25957469; DOI=10.1016/j.ajhg.2015.04.004;
RG University of Washington Center for Mendelian Genomics;
RA Chong J.X., Burrage L.C., Beck A.E., Marvin C.T., McMillin M.J.,
RA Shively K.M., Harrell T.M., Buckingham K.J., Bacino C.A., Jain M.,
RA Alanay Y., Berry S.A., Carey J.C., Gibbs R.A., Lee B.H., Krakow D.,
RA Shendure J., Nickerson D.A., Bamshad M.J.;
RT "Autosomal-dominant multiple pterygium syndrome is caused by mutations in
RT MYH3.";
RL Am. J. Hum. Genet. 96:841-849(2015).
RN [10]
RP INVOLVEMENT IN CPSFS1A, AND VARIANTS CPSFS1A ARG-333 AND PRO-1344.
RX PubMed=27381093; DOI=10.1038/ejhg.2016.84;
RA Carapito R., Goldenberg A., Paul N., Pichot A., David A., Hamel A.,
RA Dumant-Forest C., Leroux J., Ory B., Isidor B., Bahram S.;
RT "Protein-altering MYH3 variants are associated with a spectrum of
RT phenotypes extending to spondylocarpotarsal synostosis syndrome.";
RL Eur. J. Hum. Genet. 24:1746-1751(2016).
RN [11]
RP INVOLVEMENT IN CPSFS1B, AND VARIANT CPSFS1B 47-TYR--GLU-1940 DEL.
RX PubMed=29805041; DOI=10.1016/j.ajhg.2018.04.008;
RA Cameron-Christie S.R., Wells C.F., Simon M., Wessels M., Tang C.Z.N.,
RA Wei W., Takei R., Aarts-Tesselaar C., Sandaradura S., Sillence D.O.,
RA Cordier M.P., Veenstra-Knol H.E., Cassina M., Ludwig K., Trevisson E.,
RA Bahlo M., Markie D.M., Jenkins Z.A., Robertson S.P.;
RT "Recessive spondylocarpotarsal synostosis syndrome due to compound
RT heterozygosity for variants in MYH3.";
RL Am. J. Hum. Genet. 102:1115-1125(2018).
RN [12]
RP VARIANT CPSFS1A VAL-287.
RX PubMed=29314551; DOI=10.1002/ajmg.a.38593;
RA Scala M., Accogli A., De Grandis E., Allegri A., Bagowski C.P.,
RA Shoukier M., Maghnie M., Capra V.;
RT "A novel pathogenic MYH3 mutation in a child with Sheldon-Hall syndrome and
RT vertebral fusions.";
RL Am. J. Med. Genet. A 176:663-667(2018).
CC -!- FUNCTION: Muscle contraction.
CC -!- SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy
CC chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2
CC regulatory light chain subunits (MLC-2).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the
CC myofibrils.
CC -!- TISSUE SPECIFICITY: Expressed in fetal bone, thymus, placenta, heart,
CC brain, and liver. {ECO:0000269|PubMed:25957469}.
CC -!- DEVELOPMENTAL STAGE: Abundantly present in fetal skeletal muscle and
CC not present or barely detectable in heart and adult skeletal muscle.
CC -!- DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles
CC of a 28-residue repeat pattern composed of 4 heptapeptides,
CC characteristic for alpha-helical coiled coils.
CC -!- DOMAIN: Limited proteolysis of myosin heavy chain produces 1 light
CC meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further
CC cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment
CC (S2). {ECO:0000305}.
CC -!- DISEASE: Arthrogryposis, distal, 2A (DA2A) [MIM:193700]: A form of
CC distal arthrogryposis, a disease characterized by congenital joint
CC contractures that mainly involve two or more distal parts of the limbs,
CC in the absence of a primary neurological or muscle disease. DA2A is
CC characterized by contractures of the hands and feet, oropharyngeal
CC abnormalities, scoliosis, and a distinctive face that includes a very
CC small oral orifice, puckered lips, and a H-shaped dimple of the chin.
CC {ECO:0000269|PubMed:16642020, ECO:0000269|PubMed:18695058}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Arthrogryposis, distal, 2B3 (DA2B3) [MIM:618436]: A form of
CC distal arthrogryposis, a disease characterized by congenital joint
CC contractures that mainly involve two or more distal parts of the limbs,
CC in the absence of a primary neurological or muscle disease. Distal
CC arthrogryposis type 2 is characterized by contractures of the hands and
CC feet, and a distinctive face characterized by prominent nasolabial
CC folds, small mouth and downslanting palpebral fissures. DA2B3
CC inheritance is autosomal dominant. {ECO:0000269|PubMed:16642020,
CC ECO:0000269|PubMed:18695058}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Contractures, pterygia, and spondylocarpotarsal fusion
CC syndrome 1A (CPSFS1A) [MIM:178110]: An autosomal dominant disease
CC characterized by contractures of proximal and distal joints, pterygia
CC involving the neck, axillae, elbows, and/or knees, as well as variable
CC vertebral, carpal, and tarsal fusions and short stature. Progression of
CC vertebral fusions has been observed, and inter- and intrafamilial
CC variability has been reported. {ECO:0000269|PubMed:25957469,
CC ECO:0000269|PubMed:27381093, ECO:0000269|PubMed:29314551}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Contractures, pterygia, and spondylocarpotarsal fusion
CC syndrome 1B (CPSFS1B) [MIM:618469]: An autosomal recessive disease
CC characterized by contractures affecting proximal and distal joints,
CC vertebral fusions and scoliosis, carpal and tarsal fusions as well as
CC webbing of the skin (pterygium) involving the neck, elbows, fingers,
CC and/or knees. Other features include facial dysmorphism, short neck,
CC and absent finger flexion creases. Inter- and intrafamilial variability
CC has been observed. {ECO:0000269|PubMed:29805041}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents a conventional myosin. This protein should not be
CC confused with the unconventional myosin-3 (MYO3). {ECO:0000305}.
CC -!- CAUTION: Variants Ala-1622 and Val-1637 have been originally reported
CC as DA2B3 pathogenic mutations (PubMed:16642020). These variants are now
CC thought to be polymorphisms on the basis of additional family
CC information and frequencies in large databases of control populations
CC (PubMed:25957469). {ECO:0000269|PubMed:16642020,
CC ECO:0000303|PubMed:25957469}.
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DR EMBL; X13988; CAA32167.1; -; mRNA.
DR EMBL; AC002347; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X13100; CAA31492.1; -; mRNA.
DR EMBL; X51593; CAA35942.1; -; mRNA.
DR EMBL; X15696; CAA33731.1; -; mRNA.
DR CCDS; CCDS11157.1; -.
DR PIR; S04090; S04090.
DR RefSeq; NP_002461.2; NM_002470.3.
DR RefSeq; XP_011522172.1; XM_011523870.2.
DR RefSeq; XP_011522173.1; XM_011523871.2.
DR AlphaFoldDB; P11055; -.
DR SMR; P11055; -.
DR BioGRID; 110706; 44.
DR IntAct; P11055; 19.
DR MINT; P11055; -.
DR STRING; 9606.ENSP00000464317; -.
DR iPTMnet; P11055; -.
DR PhosphoSitePlus; P11055; -.
DR BioMuta; MYH3; -.
DR DMDM; 251757455; -.
DR EPD; P11055; -.
DR jPOST; P11055; -.
DR MassIVE; P11055; -.
DR MaxQB; P11055; -.
DR PaxDb; P11055; -.
DR PeptideAtlas; P11055; -.
DR PRIDE; P11055; -.
DR ProteomicsDB; 52691; -.
DR Antibodypedia; 12917; 116 antibodies from 29 providers.
DR DNASU; 4621; -.
DR Ensembl; ENST00000583535.6; ENSP00000464317.1; ENSG00000109063.15.
DR GeneID; 4621; -.
DR KEGG; hsa:4621; -.
DR MANE-Select; ENST00000583535.6; ENSP00000464317.1; NM_002470.4; NP_002461.2.
DR UCSC; uc002gmq.3; human.
DR CTD; 4621; -.
DR DisGeNET; 4621; -.
DR GeneCards; MYH3; -.
DR HGNC; HGNC:7573; MYH3.
DR HPA; ENSG00000109063; Tissue enhanced (prostate, seminal vesicle, skeletal muscle).
DR MalaCards; MYH3; -.
DR MIM; 160720; gene.
DR MIM; 178110; phenotype.
DR MIM; 193700; phenotype.
DR MIM; 618436; phenotype.
DR MIM; 618469; phenotype.
DR neXtProt; NX_P11055; -.
DR OpenTargets; ENSG00000109063; -.
DR Orphanet; 65743; Autosomal dominant multiple pterygium syndrome.
DR Orphanet; 2990; Autosomal recessive multiple pterygium syndrome.
DR Orphanet; 1146; Distal arthrogryposis type 1.
DR Orphanet; 2053; Freeman-Sheldon syndrome.
DR Orphanet; 1147; Sheldon-Hall syndrome.
DR Orphanet; 3275; Spondylocarpotarsal synostosis.
DR PharmGKB; PA31370; -.
DR VEuPathDB; HostDB:ENSG00000109063; -.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000161575; -.
DR HOGENOM; CLU_000192_8_0_1; -.
DR InParanoid; P11055; -.
DR OMA; RMVIHES; -.
DR OrthoDB; 47111at2759; -.
DR PhylomeDB; P11055; -.
DR TreeFam; TF314375; -.
DR PathwayCommons; P11055; -.
DR Reactome; R-HSA-390522; Striated Muscle Contraction.
DR SignaLink; P11055; -.
DR SIGNOR; P11055; -.
DR BioGRID-ORCS; 4621; 7 hits in 1068 CRISPR screens.
DR ChiTaRS; MYH3; human.
DR GeneWiki; MYH3; -.
DR GenomeRNAi; 4621; -.
DR Pharos; P11055; Tbio.
DR PRO; PR:P11055; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P11055; protein.
DR Bgee; ENSG00000109063; Expressed in left testis and 121 other tissues.
DR Genevisible; P11055; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005859; C:muscle myosin complex; NAS:BHF-UCL.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0030017; C:sarcomere; NAS:BHF-UCL.
DR GO; GO:0051015; F:actin filament binding; IMP:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:BHF-UCL.
DR GO; GO:0005516; F:calmodulin binding; NAS:BHF-UCL.
DR GO; GO:0000146; F:microfilament motor activity; IMP:BHF-UCL.
DR GO; GO:0017018; F:myosin phosphatase activity; TAS:Reactome.
DR GO; GO:0030048; P:actin filament-based movement; NAS:UniProtKB.
DR GO; GO:0046034; P:ATP metabolic process; IMP:BHF-UCL.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IC:BHF-UCL.
DR GO; GO:0060325; P:face morphogenesis; IC:BHF-UCL.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0030049; P:muscle filament sliding; TAS:Reactome.
DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
DR GO; GO:0045214; P:sarcomere organization; NAS:BHF-UCL.
DR GO; GO:0003009; P:skeletal muscle contraction; IMP:BHF-UCL.
DR CDD; cd14913; MYSc_Myh3; 1.
DR Gene3D; 1.20.5.370; -; 4.
DR Gene3D; 2.30.30.360; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR002928; Myosin_tail.
DR InterPro; IPR036000; MYSc_Myh3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014751; XRCC4-like_C.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil; Cytoplasm;
KW Disease variant; Methylation; Motor protein; Muscle protein; Myosin;
KW Nucleotide-binding; Reference proteome; Thick filament.
FT CHAIN 1..1940
FT /note="Myosin-3"
FT /id="PRO_0000123394"
FT DOMAIN 33..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 86..779
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 782..811
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 656..678
FT /note="Actin-binding"
FT REGION 758..772
FT /note="Actin-binding"
FT COILED 840..1933
FT /evidence="ECO:0000255"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 130
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000255"
FT VARIANT 47..1940
FT /note="Missing (in CPSFS1B)"
FT /evidence="ECO:0000269|PubMed:29805041"
FT /id="VAR_082274"
FT VARIANT 178
FT /note="T -> I (in DA2A and DA2B3; dbSNP:rs121913619)"
FT /evidence="ECO:0000269|PubMed:16642020,
FT ECO:0000269|PubMed:18695058"
FT /id="VAR_030370"
FT VARIANT 234
FT /note="A -> T (in DA2B3; dbSNP:rs121913623)"
FT /evidence="ECO:0000269|PubMed:18695058"
FT /id="VAR_082275"
FT VARIANT 243
FT /note="Missing (in CPSFS1A; dbSNP:rs1555527166)"
FT /evidence="ECO:0000269|PubMed:25957469"
FT /id="VAR_074668"
FT VARIANT 261
FT /note="S -> F (in DA2B3; dbSNP:rs1597490381)"
FT /evidence="ECO:0000269|PubMed:16642020"
FT /id="VAR_030371"
FT VARIANT 287
FT /note="F -> V (in CPSFS1A; dbSNP:rs1567560080)"
FT /evidence="ECO:0000269|PubMed:29314551"
FT /id="VAR_082276"
FT VARIANT 292
FT /note="S -> C (in DA2B3; unknown pathological significance;
FT dbSNP:rs139480342)"
FT /evidence="ECO:0000269|PubMed:16642020"
FT /id="VAR_030372"
FT VARIANT 333
FT /note="T -> R (in CPSFS1A; dbSNP:rs1567559562)"
FT /evidence="ECO:0000269|PubMed:27381093"
FT /id="VAR_082277"
FT VARIANT 375
FT /note="E -> K (in DA2B3; unknown pathological significance;
FT dbSNP:rs121913621)"
FT /evidence="ECO:0000269|PubMed:16642020"
FT /id="VAR_030373"
FT VARIANT 462
FT /note="D -> G (in DA2B3; unknown pathological significance;
FT dbSNP:rs121913622)"
FT /evidence="ECO:0000269|PubMed:18695058"
FT /id="VAR_082278"
FT VARIANT 498
FT /note="E -> G (in DA2A)"
FT /evidence="ECO:0000269|PubMed:16642020"
FT /id="VAR_030374"
FT VARIANT 517
FT /note="D -> Y (in DA2B3; unknown pathological significance;
FT dbSNP:rs1597488252)"
FT /evidence="ECO:0000269|PubMed:16642020"
FT /id="VAR_030375"
FT VARIANT 583
FT /note="Y -> S (in DA2A; dbSNP:rs1597488038)"
FT /evidence="ECO:0000269|PubMed:16642020"
FT /id="VAR_030376"
FT VARIANT 672
FT /note="R -> C (in DA2A; dbSNP:rs121913618)"
FT /evidence="ECO:0000269|PubMed:16642020"
FT /id="VAR_030377"
FT VARIANT 672
FT /note="R -> H (in DA2A; dbSNP:rs121913617)"
FT /evidence="ECO:0000269|PubMed:16642020"
FT /id="VAR_030378"
FT VARIANT 769
FT /note="G -> V (in DA2B3)"
FT /evidence="ECO:0000269|PubMed:16642020"
FT /id="VAR_030379"
FT VARIANT 825
FT /note="V -> D (in DA2A; dbSNP:rs121913620)"
FT /evidence="ECO:0000269|PubMed:16642020"
FT /id="VAR_030380"
FT VARIANT 838
FT /note="K -> E (in DA2B3)"
FT /evidence="ECO:0000269|PubMed:16642020"
FT /id="VAR_030381"
FT VARIANT 841
FT /note="Missing (in DA2B3)"
FT /evidence="ECO:0000269|PubMed:16642020"
FT /id="VAR_030382"
FT VARIANT 1003
FT /note="A -> V (in dbSNP:rs34088014)"
FT /id="VAR_056173"
FT VARIANT 1072
FT /note="N -> NN (in CPSFS1A)"
FT /evidence="ECO:0000269|PubMed:25957469"
FT /id="VAR_074669"
FT VARIANT 1075
FT /note="Q -> P (in CPSFS1A; dbSNP:rs796051884)"
FT /evidence="ECO:0000269|PubMed:25957469"
FT /id="VAR_074670"
FT VARIANT 1137
FT /note="R -> C (in dbSNP:rs12941197)"
FT /id="VAR_030196"
FT VARIANT 1192
FT /note="A -> T (in dbSNP:rs2285477)"
FT /evidence="ECO:0000269|PubMed:1691980,
FT ECO:0000269|PubMed:2726495, ECO:0000269|PubMed:2771643,
FT ECO:0000269|PubMed:2806546"
FT /id="VAR_030197"
FT VARIANT 1313
FT /note="T -> I (in dbSNP:rs35230241)"
FT /id="VAR_056174"
FT VARIANT 1344
FT /note="L -> P (in CPSFS1A; unknown pathological
FT significance; dbSNP:rs1567553806)"
FT /evidence="ECO:0000269|PubMed:27381093"
FT /id="VAR_082279"
FT VARIANT 1622
FT /note="D -> A (originally found in DA2B3 patients;
FT dbSNP:rs1446303362)"
FT /evidence="ECO:0000269|PubMed:16642020,
FT ECO:0000303|PubMed:25957469"
FT /id="VAR_030383"
FT VARIANT 1637
FT /note="A -> V (originally found in DA2B3 patients;
FT dbSNP:rs34165480)"
FT /evidence="ECO:0000269|PubMed:16642020,
FT ECO:0000303|PubMed:25957469"
FT /id="VAR_030384"
FT CONFLICT 327
FT /note="A -> R (in Ref. 1; CAA32167)"
FT /evidence="ECO:0000305"
FT CONFLICT 732
FT /note="P -> L (in Ref. 1; CAA32167)"
FT /evidence="ECO:0000305"
FT CONFLICT 1331
FT /note="A -> G (in Ref. 4; CAA35942)"
FT /evidence="ECO:0000305"
FT CONFLICT 1391..1392
FT /note="KK -> QE (in Ref. 1; CAA32167 and 3; CAA31492)"
FT /evidence="ECO:0000305"
FT CONFLICT 1608..1609
FT /note="SR -> RA (in Ref. 4; CAA35942)"
FT /evidence="ECO:0000305"
FT CONFLICT 1663..1664
FT /note="RG -> QT (in Ref. 3; CAA31492)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1940 AA; 223905 MW; B7D6AF219E88E5C8 CRC64;
MSSDTEMEVF GIAAPFLRKS EKERIEAQNQ PFDAKTYCFV VDSKEEYAKG KIKSSQDGKV
TVETEDNRTL VVKPEDVYAM NPPKFDRIED MAMLTHLNEP AVLYNLKDRY TSWMIYTYSG
LFCVTVNPYK WLPVYNPEVV EGYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
SGAGKTVNTK RVIQYFATIA ATGDLAKKKD SKMKGTLEDQ IISANPLLEA FGNAKTVRND
NSSRFGKFIR IHFGTTGKLA SADIETYLLE KSRVTFQLKA ERSYHIFYQI LSNKKPELIE
LLLITTNPYD YPFISQGEIL VASIDDAEEL LATDSAIDIL GFTPEEKSGL YKLTGAVMHY
GNMKFKQKQR EEQAEPDGTE VADKTAYLMG LNSSDLLKAL CFPRVKVGNE YVTKGQTVDQ
VHHAVNALSK SVYEKLFLWM VTRINQQLDT KLPRQHFIGV LDIAGFEIFE YNSLEQLCIN
FTNEKLQQFF NHHMFVLEQE EYKKEGIEWT FIDFGMDLAA CIELIEKPMG IFSILEEECM
FPKATDTSFK NKLYDQHLGK SNNFQKPKVV KGRAEAHFSL IHYAGTVDYS VSGWLEKNKD
PLNETVVGLY QKSSNRLLAH LYATFATADA DSGKKKVAKK KGSSFQTVSA LFRENLNKLM
SNLRTTHPHF VRCIIPNETK TPGAMEHSLV LHQLRCNGVL EGIRICRKGF PNRILYGDFK
QRYRVLNASA IPEGQFIDSK KACEKLLASI DIDHTQYKFG HTKVFFKAGL LGTLEEMRDD
RLAKLITRTQ AVCRGFLMRV EFQKMVQRRE SIFCIQYNIR SFMNVKHWPW MKLFFKIKPL
LKSAETEKEM ATMKEEFQKT KDELAKSEAK RKELEEKLVT LVQEKNDLQL QVQAESENLL
DAEERCDQLI KAKFQLEAKI KEVTERAEDE EEINAELTAK KRKLEDECSE LKKDIDDLEL
TLAKVEKEKH ATENKVKNLT EELSGLDETI AKLTREKKAL QEAHQQALDD LQAEEDKVNS
LNKTKSKLEQ QVEDLESSLE QEKKLRVDLE RNKRKLEGDL KLAQESILDL ENDKQQLDER
LKKKDFEYCQ LQSKVEDEQT LGLQFQKKIK ELQARIEELE EEIEAERATR AKTEKQRSDY
ARELEELSER LEEAGGVTST QIELNKKREA EFLKLRRDLE EATLQHEAMV AALRKKHADS
VAELGEQIDN LQRVKQKLEK EKSEFKLEID DLSSSMESVS KSKANLEKIC RTLEDQLSEA
RGKNEEIQRS LSELTTQKSR LQTEAGELSR QLEEKESIVS QLSRSKQAFT QQTEELKRQL
EEENKAKNAL AHALQSSRHD CDLLREQYEE EQEGKAELQR ALSKANSEVA QWRTKYETDA
IQRTEELEEA KKKLAQRLQD SEEQVEAVNA KCASLEKTKQ RLQGEVEDLM VDVERANSLA
AALDKKQRNF DKVLAEWKTK CEESQAELEA SLKESRSLST ELFKLKNAYE EALDQLETVK
RENKNLEQEI ADLTEQIAEN GKTIHELEKS RKQIELEKAD IQLALEEAEA ALEHEEAKIL
RIQLELTQVK SEIDRKIAEK DEEIEQLKRN YQRTVETMQS ALDAEVRSRN EAIRLKKKME
GDLNEIEIQL SHANRQAAET LKHLRSVQGQ LKDTQLHLDD ALRGQEDLKE QLAIVERRAN
LLQAEVEELR ATLEQTERAR KLAEQELLDS NERVQLLHTQ NTSLIHTKKK LETDLMQLQS
EVEDASRDAR NAEEKAKKAI TDAAMMAEEL KKEQDTSAHL ERMKKNLEQT VKDLQHRLDE
AEQLALKGGK KQIQKLETRI RELEFELEGE QKKNTESVKG LRKYERRVKE LTYQSEEDRK
NVLRLQDLVD KLQVKVKSYK RQAEEADEQA NAHLTKFRKA QHELEEAEER ADIAESQVNK
LRAKTRDFTS SRMVVHESEE
