CF410_HUMAN
ID CF410_HUMAN Reviewed; 256 AA.
AC O43822; A8MPS9; O14993; Q8N5X6; Q99837; Q99838;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Cilia- and flagella-associated protein 410 {ECO:0000312|HGNC:HGNC:1260};
DE AltName: Full=C21orf-HUMF09G8.5;
DE AltName: Full=Leucine-rich repeat-containing protein 76;
DE AltName: Full=YF5/A2;
GN Name=CFAP410 {ECO:0000312|HGNC:HGNC:1260};
GN Synonyms=C21orf2 {ECO:0000312|HGNC:HGNC:1260}, LRRC76;
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].
RC TISSUE=Lung, and Pancreas;
RX PubMed=9465297; DOI=10.1006/geno.1997.5066;
RA Scott H.S., Kyriakou D.S., Peterson P., Heino M., Tahtinen M., Krohn K.,
RA Chen H., Rossier C., Lalioti M.D., Antonarakis S.E.;
RT "Characterization of a novel gene, C21orf2, on human chromosome 21q22.3 and
RT its exclusion as the APECED gene by mutation analysis.";
RL Genomics 47:64-70(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ILE-150.
RC TISSUE=Lung;
RA Thiel C., Lehrach H., Yaspo M.-L.;
RT "Isolation of candidate genes mapping in the APECED disease (PGD type I)
RT region on Human chromosome 21q22.3.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND SHORT).
RC TISSUE=Placenta, and Teratocarcinoma;
RA Pruijn G.J.M., Misaki Y., van Venrooij W.J.;
RT "Characterization of alternatively spliced human YF5 and A2 cDNAs.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND 4).
RC TISSUE=Colon, 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 [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9325172; DOI=10.1006/bbrc.1997.7352;
RA Krohn K., Ovod V., Vilja P., Heino M., Scott H., Kyriakou D.S.,
RA Antonarakis S., Jacobs H.T., Isola J., Peterson P.;
RT "Immunochemical characterization of a novel mitochondrially located protein
RT encoded by a nuclear gene within the DFNB8/10 critical region on 21q22.3.";
RL Biochem. Biophys. Res. Commun. 238:806-810(1997).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND SER-177,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177 (ISOFORMS 3 AND 4), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [9]
RP FUNCTION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and migration.";
RL BMC Biol. 9:54-54(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND IDENTIFICATION BY
RP 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 [11]
RP FUNCTION, INTERACTION WITH NEK1, AND SUBCELLULAR LOCATION.
RX PubMed=26290490; DOI=10.1093/abbs/gmv076;
RA Fang X., Lin H., Wang X., Zuo Q., Qin J., Zhang P.;
RT "The NEK1 interactor, C21ORF2, is required for efficient DNA damage
RT repair.";
RL Acta Biochim. Biophys. Sin. 47:834-841(2015).
RN [12]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INVOLVEMENT IN RDMS, AND VARIANT
RP RDMS TYR-61.
RX PubMed=26294103; DOI=10.1136/bjophthalmol-2015-307277;
RA Khan A.O., Eisenberger T., Nagel-Wolfrum K., Wolfrum U., Bolz H.J.;
RT "C21orf2 is mutated in recessive early-onset retinal dystrophy with macular
RT staphyloma and encodes a protein that localises to the photoreceptor
RT primary cilium.";
RL Br. J. Ophthalmol. 99:1725-1731(2015).
RN [13]
RP SUBCELLULAR LOCATION, INVOLVEMENT IN SMDAX, VARIANTS SMDAX PRO-73 AND
RP PRO-224, CHARACTERIZATION OF VARIANTS SMDAX PRO-73 AND PRO-224,
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH NECK1
RP AND SPATA7, AND INTERACTION WITH NECK1.
RX PubMed=26167768; DOI=10.1038/ncb3201;
RG UK10K Consortium;
RG University of Washington Center for Mendelian Genomics;
RA Wheway G., Schmidts M., Mans D.A., Szymanska K., Nguyen T.M., Racher H.,
RA Phelps I.G., Toedt G., Kennedy J., Wunderlich K.A., Sorusch N.,
RA Abdelhamed Z.A., Natarajan S., Herridge W., van Reeuwijk J., Horn N.,
RA Boldt K., Parry D.A., Letteboer S.J., Roosing S., Adams M., Bell S.M.,
RA Bond J., Higgins J., Morrison E.E., Tomlinson D.C., Slaats G.G.,
RA van Dam T.J., Huang L., Kessler K., Giessl A., Logan C.V., Boyle E.A.,
RA Shendure J., Anazi S., Aldahmesh M., Al Hazzaa S., Hegele R.A., Ober C.,
RA Frosk P., Mhanni A.A., Chodirker B.N., Chudley A.E., Lamont R.,
RA Bernier F.P., Beaulieu C.L., Gordon P., Pon R.T., Donahue C.,
RA Barkovich A.J., Wolf L., Toomes C., Thiel C.T., Boycott K.M., McKibbin M.,
RA Inglehearn C.F., Stewart F., Omran H., Huynen M.A., Sergouniotis P.I.,
RA Alkuraya F.S., Parboosingh J.S., Innes A.M., Willoughby C.E., Giles R.H.,
RA Webster A.R., Ueffing M., Blacque O., Gleeson J.G., Wolfrum U.,
RA Beales P.L., Gibson T., Doherty D., Mitchison H.M., Roepman R.,
RA Johnson C.A.;
RT "An siRNA-based functional genomics screen for the identification of
RT regulators of ciliogenesis and ciliopathy genes.";
RL Nat. Cell Biol. 17:1074-1087(2015).
RN [14]
RP SUBCELLULAR LOCATION, VARIANTS SMDAX HIS-107 AND MET-111, VARIANT RDMS
RP CYS-107, AND CHARACTERIZATION OF VARIANTS SMDAX HIS-107 AND MET-111.
RX PubMed=27548899; DOI=10.1167/iovs.16-19450;
RA Suga A., Mizota A., Kato M., Kuniyoshi K., Yoshitake K., Sultan W.,
RA Yamazaki M., Shimomura Y., Ikeo K., Tsunoda K., Iwata T.;
RT "Identification of novel mutations in the LRR-Cap domain of C21orf2 in
RT Japanese patients with retinitis pigmentosa and Cone-Rod Dystrophy.";
RL Invest. Ophthalmol. Vis. Sci. 57:4255-4263(2016).
RN [15]
RP TISSUE SPECIFICITY, INVOLVEMENT IN SMDAX, AND VARIANTS SMDAX PRO-73;
RP HIS-107 AND LEU-116.
RX PubMed=26974433; DOI=10.1371/journal.pone.0150555;
RA Wang Z., Iida A., Miyake N., Nishiguchi K.M., Fujita K., Nakazawa T.,
RA Alswaid A., Albalwi M.A., Kim O.H., Cho T.J., Lim G.Y., Isidor B.,
RA David A., Rustad C.F., Merckoll E., Westvik J., Stattin E.L.,
RA Grigelioniene G., Kou I., Nakajima M., Ohashi H., Smithson S.,
RA Matsumoto N., Nishimura G., Ikegawa S.;
RT "Axial spondylometaphyseal dysplasia is caused by C21orf2 mutations.";
RL PLoS ONE 11:E0150555-E0150555(2016).
RN [16]
RP VARIANT SMDAX PRO-73.
RX PubMed=28422394; DOI=10.1002/ajmg.a.38215;
RA McInerney-Leo A.M., Wheeler L., Marshall M.S., Anderson L.K., Zankl A.,
RA Brown M.A., Leo P.J., Wicking C., Duncan E.L.;
RT "Homozygous variant in C21orf2 in a case of Jeune syndrome with severe
RT thoracic involvement: Extending the phenotypic spectrum.";
RL Am. J. Med. Genet. A 173:1698-1704(2017).
CC -!- FUNCTION: Plays a role in cilia formation and/or maintenance (By
CC similarity). Plays a role in the regulation of cell morphology and
CC cytoskeletal organization (PubMed:21834987). Involved in DNA damage
CC repair (PubMed:26290490). {ECO:0000250|UniProtKB:Q8C6G1,
CC ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:26290490}.
CC -!- SUBUNIT: Found in a complex with CFAP410, NEK1 and SPATA7
CC (PubMed:26167768). Interacts with NEK1 (PubMed:26290490,
CC PubMed:26167768). {ECO:0000269|PubMed:26167768,
CC ECO:0000269|PubMed:26290490}.
CC -!- INTERACTION:
CC O43822; O00244: ATOX1; NbExp=3; IntAct=EBI-2835332, EBI-10179267;
CC O43822; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-2835332, EBI-10172181;
CC O43822-4; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-11943144, EBI-2548508;
CC O43822-4; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-11943144, EBI-742688;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9325172}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:26167768, ECO:0000269|PubMed:26294103}. Cell
CC projection, cilium, photoreceptor outer segment
CC {ECO:0000269|PubMed:27548899}. Cytoplasm {ECO:0000269|PubMed:26290490}.
CC Note=Colocalizes with NEK1 and SPATA7 at the basal body.
CC {ECO:0000269|PubMed:26167768}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=Long;
CC IsoId=O43822-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=O43822-2; Sequence=VSP_004138, VSP_004139;
CC Name=3;
CC IsoId=O43822-3; Sequence=VSP_047417;
CC Name=4;
CC IsoId=O43822-4; Sequence=VSP_047417, VSP_047418;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:26974433, PubMed:9325172).
CC Expressed in the retina (PubMed:26294103).
CC -!- DISEASE: Retinal dystrophy with or without macular staphyloma (RDMS)
CC [MIM:617547]: An ocular disorder characterized by decreased vision
CC which worsen over time, and dystrophic changes in the retina, such as
CC retinal pigment epithelium mottling and vessel narrowing. Macular
CC staphyloma, without high myopia, is present in some patients.
CC {ECO:0000269|PubMed:26294103, ECO:0000269|PubMed:27548899}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Spondylometaphyseal dysplasia, axial (SMDAX) [MIM:602271]: A
CC form of spondylometaphyseal dysplasia, a group of short stature
CC disorders distinguished by abnormalities in the vertebrae and the
CC metaphyses of the tubular bones. SMDAX is characterized by metaphyseal
CC changes of truncal-juxtatruncal bones, including the proximal femora.
CC Main clinical features are postnatal growth failure, rhizomelic short
CC stature in early childhood evolving into short trunk in late childhood,
CC and thoracic hypoplasia that may cause mild to moderate respiratory
CC problems in the neonatal period and later susceptibility to airway
CC infection. Impaired visual acuity comes to medical attention in early
CC life and function rapidly deteriorates. Retinal changes are diagnosed
CC as retinitis pigmentosa or pigmentary retinal degeneration on
CC fundoscopic examination and cone-rod dystrophy on electroretinogram.
CC The radiological hallmarks include short ribs with flared, cupped
CC anterior ends, mild spondylar dysplasia, lacy iliac crests, and
CC metaphyseal irregularities essentially confined to the proximal femora.
CC {ECO:0000269|PubMed:26167768, ECO:0000269|PubMed:26974433,
CC ECO:0000269|PubMed:27548899, ECO:0000269|PubMed:28422394}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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DR EMBL; Y11392; CAA72202.1; -; mRNA.
DR EMBL; Z93322; CAB07532.1; -; mRNA.
DR EMBL; U84569; AAB46590.1; -; mRNA.
DR EMBL; U84570; AAB46591.1; -; mRNA.
DR EMBL; AP001062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001754; BAA95562.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09432.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09434.1; -; Genomic_DNA.
DR EMBL; BC031300; AAH31300.1; -; mRNA.
DR EMBL; BC072012; AAH72012.1; -; mRNA.
DR CCDS; CCDS13709.1; -. [O43822-1]
DR CCDS; CCDS59444.1; -. [O43822-4]
DR CCDS; CCDS59445.1; -. [O43822-3]
DR RefSeq; NP_001258369.1; NM_001271440.1. [O43822-3]
DR RefSeq; NP_001258370.1; NM_001271441.1. [O43822-4]
DR RefSeq; NP_001258371.1; NM_001271442.1.
DR RefSeq; NP_004919.1; NM_004928.2. [O43822-1]
DR AlphaFoldDB; O43822; -.
DR SMR; O43822; -.
DR BioGRID; 107211; 46.
DR IntAct; O43822; 31.
DR iPTMnet; O43822; -.
DR PhosphoSitePlus; O43822; -.
DR BioMuta; C21orf2; -.
DR EPD; O43822; -.
DR jPOST; O43822; -.
DR MassIVE; O43822; -.
DR MaxQB; O43822; -.
DR PaxDb; O43822; -.
DR PeptideAtlas; O43822; -.
DR PRIDE; O43822; -.
DR ProteomicsDB; 49187; -. [O43822-1]
DR ProteomicsDB; 49188; -. [O43822-2]
DR ProteomicsDB; 72105; -.
DR Antibodypedia; 24213; 159 antibodies from 21 providers.
DR DNASU; 755; -.
DR Ensembl; ENST00000325223.7; ENSP00000317302.7; ENSG00000160226.16. [O43822-3]
DR Ensembl; ENST00000339818.9; ENSP00000344566.4; ENSG00000160226.16. [O43822-1]
DR Ensembl; ENST00000397956.7; ENSP00000381047.3; ENSG00000160226.16. [O43822-4]
DR GeneID; 755; -.
DR KEGG; hsa:755; -.
DR MANE-Select; ENST00000339818.9; ENSP00000344566.4; NM_004928.3; NP_004919.1.
DR UCSC; uc002zep.2; human. [O43822-1]
DR CTD; 755; -.
DR DisGeNET; 755; -.
DR GeneCards; CFAP410; -.
DR HGNC; HGNC:1260; CFAP410.
DR HPA; ENSG00000160226; Low tissue specificity.
DR MalaCards; CFAP410; -.
DR MIM; 602271; phenotype.
DR MIM; 603191; gene.
DR MIM; 617547; phenotype.
DR neXtProt; NX_O43822; -.
DR OpenTargets; ENSG00000160226; -.
DR Orphanet; 803; Amyotrophic lateral sclerosis.
DR Orphanet; 1872; Cone rod dystrophy.
DR PharmGKB; PA25816; -.
DR VEuPathDB; HostDB:ENSG00000160226; -.
DR eggNOG; KOG2123; Eukaryota.
DR GeneTree; ENSGT00390000018807; -.
DR HOGENOM; CLU_062035_2_0_1; -.
DR InParanoid; O43822; -.
DR OMA; ETDCSCK; -.
DR OrthoDB; 1021585at2759; -.
DR PhylomeDB; O43822; -.
DR TreeFam; TF326666; -.
DR PathwayCommons; O43822; -.
DR SignaLink; O43822; -.
DR BioGRID-ORCS; 755; 65 hits in 1074 CRISPR screens.
DR ChiTaRS; C21orf2; human.
DR GenomeRNAi; 755; -.
DR Pharos; O43822; Tbio.
DR PRO; PR:O43822; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; O43822; protein.
DR Bgee; ENSG00000160226; Expressed in right uterine tube and 121 other tissues.
DR Genevisible; O43822; HS.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0032391; C:photoreceptor connecting cilium; ISS:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; IEA:Ensembl.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR003603; U2A'_phosphoprotein32A_C.
DR SMART; SM00446; LRRcap; 1.
DR PROSITE; PS51450; LRR; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Ciliopathy;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Disease variant;
KW DNA damage; Dwarfism; Leucine-rich repeat; Mitochondrion; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..256
FT /note="Cilia- and flagella-associated protein 410"
FT /id="PRO_0000079503"
FT REPEAT 19..40
FT /note="LRR 1"
FT REPEAT 41..62
FT /note="LRR 2"
FT REPEAT 63..84
FT /note="LRR 3"
FT DOMAIN 97..137
FT /note="LRRCT"
FT REGION 129..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_004138"
FT VAR_SEQ 49..51
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_004139"
FT VAR_SEQ 183
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_047417"
FT VAR_SEQ 214
FT /note="R -> RVSGGPLGAAAASAHCTHCTETVGREHGASQGPVGREHGASQGLEEL
FT CPRGSCVCGSVNAHTRVTRAPHGAVLAPQPLLLSWSVECGPGPCWAEGNRSHVEEVPHT
FT RPQAGLLCSDSPSVP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047418"
FT VARIANT 61
FT /note="C -> Y (in RDMS; dbSNP:rs1057518441)"
FT /evidence="ECO:0000269|PubMed:26294103"
FT /id="VAR_079180"
FT VARIANT 73
FT /note="R -> P (in SMDAX; patients may exhibit clinical
FT features overlapping with Jeune syndrome; decreased
FT function in ciliogenesis; abolishes interaction with NEK1;
FT dbSNP:rs140451304)"
FT /evidence="ECO:0000269|PubMed:26167768,
FT ECO:0000269|PubMed:26974433, ECO:0000269|PubMed:28422394"
FT /id="VAR_075924"
FT VARIANT 107
FT /note="Y -> C (in RDMS; dbSNP:rs1131690801)"
FT /evidence="ECO:0000269|PubMed:27548899"
FT /id="VAR_079181"
FT VARIANT 107
FT /note="Y -> H (in SMDAX; increases protein degradation;
FT changes protein localization; dbSNP:rs763623409)"
FT /evidence="ECO:0000269|PubMed:26974433,
FT ECO:0000269|PubMed:27548899"
FT /id="VAR_075925"
FT VARIANT 111
FT /note="V -> M (in SMDAX; increases protein degradation;
FT changes protein localization; dbSNP:rs555164150)"
FT /evidence="ECO:0000269|PubMed:27548899"
FT /id="VAR_079182"
FT VARIANT 116
FT /note="P -> L (in SMDAX; dbSNP:rs922930539)"
FT /evidence="ECO:0000269|PubMed:26974433"
FT /id="VAR_075926"
FT VARIANT 150
FT /note="T -> I (in dbSNP:rs2277809)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_016155"
FT VARIANT 153
FT /note="G -> S (in dbSNP:rs9306099)"
FT /id="VAR_050927"
FT VARIANT 224
FT /note="L -> P (in SMDAX; abolishes interaction with NEK1;
FT dbSNP:rs1114167892)"
FT /evidence="ECO:0000269|PubMed:26167768"
FT /id="VAR_075927"
FT CONFLICT 106
FT /note="R -> A (in Ref. 3; AAB46590/AAB46591)"
FT /evidence="ECO:0000305"
FT MOD_RES O43822-3:177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES O43822-4:177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
SQ SEQUENCE 256 AA; 28340 MW; D33F31EDAEA77D2A CRC64;
MKLTRKMVLT RAKASELHSV RKLNCWGSRL TDISICQEMP SLEVITLSVN SISTLEPVSR
CQRLSELYLR RNRIPSLAEL FYLKGLPRLR VLWLAENPCC GTSPHRYRMT VLRTLPRLQK
LDNQAVTEEE LSRALSEGEE ITAAPEREGT GHGGPKLCCT LSSLSSAAET GRDPLDSEEE
ATSGAQDERG LKPPSRGQFP SLSARDASSS HRGRNVLTAI LLLLRELDAE GLEAVQQTVG
SRLQALRGEE VQEHAE
