C2D1A_HUMAN
ID C2D1A_HUMAN Reviewed; 951 AA.
AC Q6P1N0; Q7Z435; Q86XV0; Q8NF89; Q9H603; Q9NXI1;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Coiled-coil and C2 domain-containing protein 1A;
DE AltName: Full=Akt kinase-interacting protein 1;
DE AltName: Full=Five prime repressor element under dual repression-binding protein 1;
DE Short=FRE under dual repression-binding protein 1;
DE Short=Freud-1;
DE AltName: Full=Putative NF-kappa-B-activating protein 023N;
GN Name=CC2D1A; Synonyms=AKI1;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RA Guo J.H., Chen L., Yu L.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung fibroblast;
RX PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y.,
RA Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.;
RT "Large-scale identification and characterization of human genes that
RT activate NF-kappaB and MAPK signaling pathways.";
RL Oncogene 22:3307-3318(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 254-606 AND 622-951 (ISOFORM 1).
RC TISSUE=Ovary;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Ovary;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [6]
RP SUBCELLULAR LOCATION, AND INVOLVEMENT IN MRT3.
RX PubMed=16033914; DOI=10.1136/jmg.2005.035709;
RA Basel-Vanagaite L., Attia R., Yahav M., Ferland R.J., Anteki L.,
RA Walsh C.A., Olender T., Straussberg R., Magal N., Taub E., Drasinover V.,
RA Alkelai A., Bercovich D., Rechavi G., Simon A.J., Shohat M.;
RT "The CC2D1A, a member of a new gene family with C2 domains, is involved in
RT autosomal recessive non-syndromic mental retardation.";
RL J. Med. Genet. 43:203-210(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-204; SER-208; SER-253 AND
RP SER-455, AND IDENTIFICATION BY 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 [10]
RP FUNCTION, PHOSPHORYLATION AT SER-208 BY CDK1, AND SUBCELLULAR LOCATION.
RX PubMed=20171170; DOI=10.1016/j.bbrc.2010.02.103;
RA Nakamura A., Naito M., Arai H., Fujita N.;
RT "Mitotic phosphorylation of Aki1 at Ser208 by cyclin B1-Cdk1 complex.";
RL Biochem. Biophys. Res. Commun. 393:872-876(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208 AND SER-455, AND
RP IDENTIFICATION BY 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-206; SER-208 AND SER-455, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-455, AND
RP IDENTIFICATION 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).
CC -!- FUNCTION: Transcription factor that binds specifically to the DRE (dual
CC repressor element) and represses HTR1A gene transcription in neuronal
CC cells. The combination of calcium and ATP specifically inactivates the
CC binding with FRE. May play a role in the altered regulation of HTR1A
CC associated with anxiety and major depression. Mediates HDAC-independent
CC repression of HTR1A promoter in neuronal cell. Performs essential
CC function in controlling functional maturation of synapses (By
CC similarity). Plays distinct roles depending on its localization. When
CC cytoplasmic, acts as a scaffold protein in the PI3K/PDK1/AKT pathway.
CC Repressor of HTR1A when nuclear. In the centrosome, regulates spindle
CC pole localization of the cohesin subunit SCC1/RAD21, thereby mediating
CC centriole cohesion during mitosis. {ECO:0000250,
CC ECO:0000269|PubMed:20171170}.
CC -!- INTERACTION:
CC Q6P1N0; Q9H444: CHMP4B; NbExp=3; IntAct=EBI-7112364, EBI-749627;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16033914}. Nucleus
CC {ECO:0000250|UniProtKB:Q66HA5}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000303|PubMed:20171170}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P1N0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P1N0-2; Sequence=VSP_019242;
CC -!- DOMAIN: The C2 domain is required for the repression. {ECO:0000250}.
CC -!- PTM: Phosphorylation on Ser-208 by CDK1 promotes spindle pole
CC localization and association with SCC1/RAD21.
CC {ECO:0000269|PubMed:20171170}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 3
CC (MRT3) [MIM:608443]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC {ECO:0000269|PubMed:16033914}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CC2D1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91029.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=BAB15464.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF536205; AAN04488.1; -; mRNA.
DR EMBL; AB097002; BAC77355.1; -; mRNA.
DR EMBL; AK000248; BAA91029.1; ALT_SEQ; mRNA.
DR EMBL; AK026371; BAB15464.1; ALT_INIT; mRNA.
DR EMBL; BC048345; AAH48345.1; -; mRNA.
DR EMBL; BC064981; AAH64981.1; -; mRNA.
DR CCDS; CCDS42512.1; -. [Q6P1N0-1]
DR RefSeq; NP_060191.3; NM_017721.4. [Q6P1N0-1]
DR RefSeq; XP_005260030.1; XM_005259973.2. [Q6P1N0-2]
DR AlphaFoldDB; Q6P1N0; -.
DR SMR; Q6P1N0; -.
DR BioGRID; 120212; 110.
DR IntAct; Q6P1N0; 40.
DR MINT; Q6P1N0; -.
DR STRING; 9606.ENSP00000313601; -.
DR GlyGen; Q6P1N0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6P1N0; -.
DR PhosphoSitePlus; Q6P1N0; -.
DR BioMuta; CC2D1A; -.
DR DMDM; 74737148; -.
DR EPD; Q6P1N0; -.
DR jPOST; Q6P1N0; -.
DR MassIVE; Q6P1N0; -.
DR MaxQB; Q6P1N0; -.
DR PaxDb; Q6P1N0; -.
DR PeptideAtlas; Q6P1N0; -.
DR PRIDE; Q6P1N0; -.
DR ProteomicsDB; 66855; -. [Q6P1N0-1]
DR ProteomicsDB; 66856; -. [Q6P1N0-2]
DR Antibodypedia; 1689; 175 antibodies from 28 providers.
DR DNASU; 54862; -.
DR Ensembl; ENST00000318003.11; ENSP00000313601.6; ENSG00000132024.18. [Q6P1N0-1]
DR Ensembl; ENST00000589606.5; ENSP00000467526.1; ENSG00000132024.18. [Q6P1N0-2]
DR Ensembl; ENST00000672017.1; ENSP00000500461.1; ENSG00000288293.1. [Q6P1N0-1]
DR Ensembl; ENST00000672339.1; ENSP00000500343.1; ENSG00000288293.1. [Q6P1N0-2]
DR GeneID; 54862; -.
DR KEGG; hsa:54862; -.
DR MANE-Select; ENST00000318003.11; ENSP00000313601.6; NM_017721.5; NP_060191.3.
DR UCSC; uc002mxo.3; human. [Q6P1N0-1]
DR CTD; 54862; -.
DR DisGeNET; 54862; -.
DR GeneCards; CC2D1A; -.
DR HGNC; HGNC:30237; CC2D1A.
DR HPA; ENSG00000132024; Low tissue specificity.
DR MalaCards; CC2D1A; -.
DR MIM; 608443; phenotype.
DR MIM; 610055; gene.
DR neXtProt; NX_Q6P1N0; -.
DR OpenTargets; ENSG00000132024; -.
DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
DR PharmGKB; PA142672197; -.
DR VEuPathDB; HostDB:ENSG00000132024; -.
DR eggNOG; KOG3837; Eukaryota.
DR GeneTree; ENSGT00390000009595; -.
DR HOGENOM; CLU_008808_0_0_1; -.
DR InParanoid; Q6P1N0; -.
DR OMA; NLAKQHY; -.
DR OrthoDB; 959801at2759; -.
DR PhylomeDB; Q6P1N0; -.
DR TreeFam; TF314229; -.
DR PathwayCommons; Q6P1N0; -.
DR SignaLink; Q6P1N0; -.
DR SIGNOR; Q6P1N0; -.
DR BioGRID-ORCS; 54862; 11 hits in 1082 CRISPR screens.
DR ChiTaRS; CC2D1A; human.
DR GeneWiki; CC2D1A; -.
DR GenomeRNAi; 54862; -.
DR Pharos; Q6P1N0; Tbio.
DR PRO; PR:Q6P1N0; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q6P1N0; protein.
DR Bgee; ENSG00000132024; Expressed in right hemisphere of cerebellum and 89 other tissues.
DR ExpressionAtlas; Q6P1N0; baseline and differential.
DR Genevisible; Q6P1N0; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:GO_Central.
DR GO; GO:1905381; P:negative regulation of snRNA transcription by RNA polymerase II; IDA:GO_Central.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd08690; C2_Freud-1; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037772; C2_Freud.
DR InterPro; IPR039725; CC2D1A/B.
DR InterPro; IPR006608; DM14.
DR PANTHER; PTHR13076; PTHR13076; 1.
DR Pfam; PF00168; C2; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00685; DM14; 4.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; DNA-binding;
KW Intellectual disability; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..951
FT /note="Coiled-coil and C2 domain-containing protein 1A"
FT /id="PRO_0000239609"
FT DOMAIN 637..771
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 80..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 346..392
FT /evidence="ECO:0000255"
FT COILED 484..517
FT /evidence="ECO:0000255"
FT COMPBIAS 83..108
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..343
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 92
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q66HA5"
FT MOD_RES 204
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 206
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 208
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:20171170,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 819
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_019242"
FT VARIANT 339
FT /note="T -> P (in dbSNP:rs11883041)"
FT /id="VAR_026670"
FT VARIANT 635
FT /note="T -> S (in dbSNP:rs2290663)"
FT /id="VAR_026671"
FT VARIANT 801
FT /note="T -> M (in dbSNP:rs2305777)"
FT /id="VAR_026672"
FT CONFLICT 646
FT /note="I -> V (in Ref. 1; AAN04488)"
FT /evidence="ECO:0000305"
FT CONFLICT 824
FT /note="K -> E (in Ref. 2; BAC77355)"
FT /evidence="ECO:0000305"
FT CONFLICT 837
FT /note="S -> P (in Ref. 2; BAC77355)"
FT /evidence="ECO:0000305"
FT CONFLICT 906
FT /note="A -> T (in Ref. 2; BAC77355)"
FT /evidence="ECO:0000305"
FT CONFLICT 943
FT /note="E -> G (in Ref. 2; BAC77355)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 951 AA; 104062 MW; 04D80124FC47729A CRC64;
MHKRKGPPGP PGRGAAAARQ LGLLVDLSPD GLMIPEDGAN DEELEAEFLA LVGGQPPALE
KLKGKGPLPM EAIEKMASLC MRDPDEDEEE GTDEDDLEAD DDLLAELNEV LGEEQKASET
PPPVAQPKPE APHPGLETTL QERLALYQTA IESARQAGDS AKMRRYDRGL KTLENLLASI
RKGNAIDEAD IPPPVAIGKG PASTPTYSPA PTQPAPRIAS APEPRVTLEG PSATAPASSP
GLAKPQMPPG PCSPGPLAQL QSRQRDYKLA ALHAKQQGDT TAAARHFRVA KSFDAVLEAL
SRGEPVDLSC LPPPPDQLPP DPPSPPSQPP TPATAPSTTE VPPPPRTLLE ALEQRMERYQ
VAAAQAKSKG DQRKARMHER IVKQYQDAIR AHKAGRAVDV AELPVPPGFP PIQGLEATKP
TQQSLVGVLE TAMKLANQDE GPEDEEDEVP KKQNSPVAPT AQPKAPPSRT PQSGSAPTAK
APPKATSTRA QQQLAFLEGR KKQLLQAALR AKQKNDVEGA KMHLRQAKGL EPMLEASRNG
LPVDITKVPP APVNKDDFAL VQRPGPGLSQ EAARRYGELT KLIRQQHEMC LNHSNQFTQL
GNITETTKFE KLAEDCKRSM DILKQAFVRG LPTPTARFEQ RTFSVIKIFP DLSSNDMLLF
IVKGINLPTP PGLSPGDLDV FVRFDFPYPN VEEAQKDKTS VIKNTDSPEF KEQFKLCINR
SHRGFRRAIQ TKGIKFEVVH KGGLFKTDRV LGTAQLKLDA LEIACEVREI LEVLDGRRPT
GGRLEVMVRI REPLTAQQLE TTTERWLVID PVPAAVPTQV AGPKGKAPPV PAPARESGNR
SARPLHSLSV LAFDQERLER KILALRQARR PVPPEVAQQY QDIMQRSQWQ RAQLEQGGVG
IRREYAAQLE RQLQFYTEAA RRLGNDGSRD AAKEALYRRN LVESELQRLR R
