MIPT3_HUMAN
ID MIPT3_HUMAN Reviewed; 691 AA.
AC Q8TDR0; Q6PCT1; Q7L8N9; Q9NRD6; Q9Y4Q1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=TRAF3-interacting protein 1;
DE AltName: Full=Interleukin-13 receptor alpha 1-binding protein 1;
DE AltName: Full=Intraflagellar transport protein 54 homolog;
DE AltName: Full=Microtubule-interacting protein associated with TRAF3;
DE Short=MIP-T3;
GN Name=TRAF3IP1; Synonyms=IFT54, MIPT3;
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 2), FUNCTION, AND INTERACTION WITH
RP IL13RA1.
RX PubMed=10791955; DOI=10.1074/jbc.m001095200;
RA Ling L., Goeddel D.V.;
RT "MIP-T3, a novel protein linking tumor necrosis factor receptor-associated
RT factor 3 to the microtubule network.";
RL J. Biol. Chem. 275:23852-23860(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION,
RP SUBCELLULAR LOCATION, REGION, AND INTERACTION WITH TRAF3.
RC TISSUE=Testis;
RX PubMed=12935900; DOI=10.1016/s0014-5793(03)00860-3;
RA Niu Y., Murata T., Watanabe K., Kawakami K., Yoshimura A., Inoue J.,
RA Puri R.K., Kobayashi N.;
RT "MIP-T3 associates with IL-13Ralpha1 and suppresses STAT6 activation in
RT response to IL-13 stimulation.";
RL FEBS Lett. 550:139-143(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT SER-228.
RC TISSUE=PNS;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 49-691 (ISOFORM 2).
RC TISSUE=Testis;
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 [7]
RP FUNCTION, INTERACTION WITH DISC1, AND REGION.
RX PubMed=12812986; DOI=10.1093/hmg/ddg162;
RA Morris J.A., Kandpal G., Ma L., Austin C.P.;
RT "DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein
RT that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of
RT interaction with mutation.";
RL Hum. Mol. Genet. 12:1591-1608(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, 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, SUBCELLULAR LOCATION, INVOLVEMENT IN SLSN9, VARIANTS SLSN9
RP SER-17; ALA-125; MET-125 AND ARG-520, AND CHARACTERIZATION OF VARIANTS
RP SLSN9 SER-17; ALA-125; MET-125 AND ARG-520.
RX PubMed=26487268; DOI=10.1038/ncomms9666;
RA Bizet A.A., Becker-Heck A., Ryan R., Weber K., Filhol E., Krug P.,
RA Halbritter J., Delous M., Lasbennes M.C., Linghu B., Oakeley E.J.,
RA Zarhrate M., Nitschke P., Garfa-Traore M., Serluca F., Yang F.,
RA Bouwmeester T., Pinson L., Cassuto E., Dubot P., Elshakhs N.A., Sahel J.A.,
RA Salomon R., Drummond I.A., Gubler M.C., Antignac C., Chibout S.,
RA Szustakowski J.D., Hildebrandt F., Lorentzen E., Sailer A.W., Benmerah A.,
RA Saint-Mezard P., Saunier S.;
RT "Mutations in TRAF3IP1/IFT54 reveal a new role for IFT proteins in
RT microtubule stabilization.";
RL Nat. Commun. 6:8666-8666(2015).
RN [12]
RP STRUCTURE BY NMR OF 1-133.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the STN_TRAF3IP1_ND domain of interleukin 13
RT receptor alpha 1-binding protein-1 [Homo sapiens].";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Plays an inhibitory role on IL13 signaling by binding to
CC IL13RA1. Involved in suppression of IL13-induced STAT6 phosphorylation,
CC transcriptional activity and DNA-binding. Recruits TRAF3 and DISC1 to
CC the microtubules. Involved in kidney development and epithelial
CC morphogenesis. Involved in the regulation of microtubule cytoskeleton
CC organization. Is a negative regulator of microtubule stability, acting
CC through the control of MAP4 levels (PubMed:26487268). Involved in
CC ciliogenesis (By similarity). {ECO:0000250|UniProtKB:Q149C2,
CC ECO:0000269|PubMed:10791955, ECO:0000269|PubMed:12812986,
CC ECO:0000269|PubMed:12935900, ECO:0000269|PubMed:26487268}.
CC -!- SUBUNIT: Component of the IFT complex B, at least composed of IFT20,
CC IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74,
CC IFT80, IFT81, and IFT88. Interacts with IFT88 (By similarity).
CC Interacts with IL13RA1 (PubMed:10791955). Binds to microtubules, TRAF3
CC and DISC1 (PubMed:12812986, PubMed:12935900). Interacts with MAP4 (By
CC similarity). {ECO:0000250|UniProtKB:Q149C2,
CC ECO:0000269|PubMed:10791955, ECO:0000269|PubMed:12812986,
CC ECO:0000269|PubMed:12935900}.
CC -!- INTERACTION:
CC Q8TDR0; Q9NRI5: DISC1; NbExp=9; IntAct=EBI-928811, EBI-529989;
CC Q8TDR0; P11142: HSPA8; NbExp=3; IntAct=EBI-928811, EBI-351896;
CC Q8TDR0; P78552: IL13RA1; NbExp=3; IntAct=EBI-928811, EBI-1391535;
CC Q8TDR0; Q13114: TRAF3; NbExp=8; IntAct=EBI-928811, EBI-357631;
CC Q8TDR0-2; Q96ES7: SGF29; NbExp=3; IntAct=EBI-11946508, EBI-743117;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12935900}. Cell projection, cilium
CC {ECO:0000269|PubMed:26487268}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:Q149C2}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q149C2}. Note=Microtubules
CC (PubMed:12935900). In the cilium, it is observed at the ciliary base,
CC ciliary transition zone and ciliary tip (PubMed:26487268).
CC {ECO:0000269|PubMed:12935900, ECO:0000269|PubMed:26487268}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TDR0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TDR0-2; Sequence=VSP_027734;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12935900}.
CC -!- DISEASE: Senior-Loken syndrome 9 (SLSN9) [MIM:616629]: A renal-retinal
CC disorder characterized by progressive wasting of the filtering unit of
CC the kidney (nephronophthisis), with or without medullary cystic renal
CC disease, and progressive eye disease. Typically this disorder becomes
CC apparent during the first year of life. {ECO:0000269|PubMed:26487268}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the TRAF3IP1 family. {ECO:0000305}.
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DR EMBL; AF230877; AAF76984.1; -; mRNA.
DR EMBL; AF242456; AAL90444.1; -; mRNA.
DR EMBL; AC012485; AAX88977.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW71157.1; -; Genomic_DNA.
DR EMBL; BC059174; AAH59174.1; -; mRNA.
DR EMBL; AL080153; CAB45744.1; -; mRNA.
DR CCDS; CCDS33415.1; -. [Q8TDR0-1]
DR CCDS; CCDS46557.1; -. [Q8TDR0-2]
DR PIR; T12536; T12536.
DR RefSeq; NP_001132962.1; NM_001139490.1. [Q8TDR0-2]
DR RefSeq; NP_056465.2; NM_015650.3. [Q8TDR0-1]
DR PDB; 2EQO; NMR; -; A=1-133.
DR PDBsum; 2EQO; -.
DR AlphaFoldDB; Q8TDR0; -.
DR SMR; Q8TDR0; -.
DR BioGRID; 117577; 92.
DR ComplexPortal; CPX-5022; IFT-B complex.
DR CORUM; Q8TDR0; -.
DR IntAct; Q8TDR0; 133.
DR STRING; 9606.ENSP00000362424; -.
DR GlyGen; Q8TDR0; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TDR0; -.
DR PhosphoSitePlus; Q8TDR0; -.
DR BioMuta; TRAF3IP1; -.
DR DMDM; 74727348; -.
DR EPD; Q8TDR0; -.
DR jPOST; Q8TDR0; -.
DR MassIVE; Q8TDR0; -.
DR MaxQB; Q8TDR0; -.
DR PaxDb; Q8TDR0; -.
DR PeptideAtlas; Q8TDR0; -.
DR PRIDE; Q8TDR0; -.
DR ProteomicsDB; 74330; -. [Q8TDR0-1]
DR ProteomicsDB; 74331; -. [Q8TDR0-2]
DR Antibodypedia; 34501; 232 antibodies from 28 providers.
DR DNASU; 26146; -.
DR Ensembl; ENST00000373327.5; ENSP00000362424.4; ENSG00000204104.12. [Q8TDR0-1]
DR Ensembl; ENST00000391993.7; ENSP00000375851.3; ENSG00000204104.12. [Q8TDR0-2]
DR GeneID; 26146; -.
DR KEGG; hsa:26146; -.
DR MANE-Select; ENST00000373327.5; ENSP00000362424.4; NM_015650.4; NP_056465.2.
DR UCSC; uc002vye.4; human. [Q8TDR0-1]
DR CTD; 26146; -.
DR DisGeNET; 26146; -.
DR GeneCards; TRAF3IP1; -.
DR HGNC; HGNC:17861; TRAF3IP1.
DR HPA; ENSG00000204104; Low tissue specificity.
DR MalaCards; TRAF3IP1; -.
DR MIM; 607380; gene.
DR MIM; 616629; phenotype.
DR neXtProt; NX_Q8TDR0; -.
DR OpenTargets; ENSG00000204104; -.
DR Orphanet; 3156; Senior-Loken syndrome.
DR Orphanet; 93269; Short rib-polydactyly syndrome, Majewski type.
DR PharmGKB; PA134943602; -.
DR VEuPathDB; HostDB:ENSG00000204104; -.
DR eggNOG; KOG3809; Eukaryota.
DR GeneTree; ENSGT00720000108822; -.
DR HOGENOM; CLU_023216_0_0_1; -.
DR InParanoid; Q8TDR0; -.
DR OMA; FLQKMID; -.
DR OrthoDB; 1008610at2759; -.
DR PhylomeDB; Q8TDR0; -.
DR TreeFam; TF315473; -.
DR PathwayCommons; Q8TDR0; -.
DR Reactome; R-HSA-5620924; Intraflagellar transport.
DR SignaLink; Q8TDR0; -.
DR BioGRID-ORCS; 26146; 19 hits in 1080 CRISPR screens.
DR ChiTaRS; TRAF3IP1; human.
DR EvolutionaryTrace; Q8TDR0; -.
DR GenomeRNAi; 26146; -.
DR Pharos; Q8TDR0; Tbio.
DR PRO; PR:Q8TDR0; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8TDR0; protein.
DR Bgee; ENSG00000204104; Expressed in oocyte and 183 other tissues.
DR ExpressionAtlas; Q8TDR0; baseline and differential.
DR Genevisible; Q8TDR0; HS.
DR GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR GO; GO:0097546; C:ciliary base; IDA:UniProtKB.
DR GO; GO:0097542; C:ciliary tip; IDA:UniProtKB.
DR GO; GO:0035869; C:ciliary transition zone; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; TAS:Reactome.
DR GO; GO:0030992; C:intraciliary transport particle B; IPI:ComplexPortal.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0035720; P:intraciliary anterograde transport; IC:ComplexPortal.
DR GO; GO:0042073; P:intraciliary transport; IBA:GO_Central.
DR GO; GO:0001822; P:kidney development; IMP:UniProtKB.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; IDA:UniProtKB.
DR GO; GO:0050687; P:negative regulation of defense response to virus; IMP:CACAO.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:CACAO.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IMP:CACAO.
DR GO; GO:0032480; P:negative regulation of type I interferon production; IMP:CACAO.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:UniProtKB.
DR Gene3D; 1.10.418.50; -; 1.
DR InterPro; IPR018799; TRAF3IP1.
DR InterPro; IPR041476; TRAF3IP1_C.
DR InterPro; IPR040468; TRAF3IP1_N.
DR InterPro; IPR042576; TRAF3IP1_N_sf.
DR PANTHER; PTHR31363; PTHR31363; 1.
DR Pfam; PF10243; MIP-T3; 1.
DR Pfam; PF17749; MIP-T3_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Ciliopathy; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disease variant; Leber congenital amaurosis; Nephronophthisis;
KW Phosphoprotein; Reference proteome; Senior-Loken syndrome.
FT CHAIN 1..691
FT /note="TRAF3-interacting protein 1"
FT /id="PRO_0000299544"
FT REGION 1..323
FT /note="Abolishes microtubules-binding when missing"
FT REGION 136..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..691
FT /note="DISC1-interaction domain"
FT COILED 571..666
FT /evidence="ECO:0000255"
FT COMPBIAS 149..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q149C2"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 355..420
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10791955,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_027734"
FT VARIANT 17
FT /note="I -> S (in SLSN9; results in altered folding of the
FT N-terminus; does not affect interaction with IFT20; loss of
FT interaction with MAP4)"
FT /evidence="ECO:0000269|PubMed:26487268"
FT /id="VAR_075068"
FT VARIANT 125
FT /note="V -> A (in SLSN9; results in altered folding of the
FT N-terminus; does not affect interaction with IFT20; loss of
FT interaction with MAP4; dbSNP:rs886037896)"
FT /evidence="ECO:0000269|PubMed:26487268"
FT /id="VAR_075069"
FT VARIANT 125
FT /note="V -> M (in SLSN9; results in altered folding of the
FT N-terminus; does not localize to the ciliary tip and
FT transition zone; does not affect interaction with IFT20;
FT loss of interaction with MAP4; dbSNP:rs886037898)"
FT /evidence="ECO:0000269|PubMed:26487268"
FT /id="VAR_075070"
FT VARIANT 228
FT /note="N -> S (in dbSNP:rs3769110)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_034841"
FT VARIANT 239
FT /note="R -> W (in dbSNP:rs34723381)"
FT /id="VAR_034842"
FT VARIANT 295
FT /note="K -> N (in dbSNP:rs12464423)"
FT /id="VAR_051185"
FT VARIANT 416
FT /note="T -> S (in dbSNP:rs58277463)"
FT /id="VAR_061685"
FT VARIANT 520
FT /note="M -> R (in SLSN9; does not localize to the ciliary
FT tip; dbSNP:rs750055952)"
FT /evidence="ECO:0000269|PubMed:26487268"
FT /id="VAR_075071"
FT VARIANT 620
FT /note="M -> L (in dbSNP:rs3739070)"
FT /id="VAR_034843"
FT HELIX 4..16
FT /evidence="ECO:0007829|PDB:2EQO"
FT TURN 24..28
FT /evidence="ECO:0007829|PDB:2EQO"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:2EQO"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:2EQO"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:2EQO"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:2EQO"
FT HELIX 66..84
FT /evidence="ECO:0007829|PDB:2EQO"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:2EQO"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:2EQO"
FT HELIX 101..116
FT /evidence="ECO:0007829|PDB:2EQO"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:2EQO"
SQ SEQUENCE 691 AA; 78632 MW; 0675AA0E5319D2EB CRC64;
MNAAVVRRTQ EALGKVIRRP PLTEKLLSKP PFRYLHDIIT EVIRMTGFMK GLYTDAEMKS
DNVKDKDAKI SFLQKAIDVV VMVSGEPLLA KPARIVAGHE PERTNELLQI IGKCCLNKLS
SDDAVRRVLA GEKGEVKGRA SLTSRSQELD NKNVREEESR VHKNTEDRGD AEIKERSTSR
DRKQKEELKE DRKPREKDKD KEKAKENGGN RHREGERERA KARARPDNER QKDRGNRERD
RDSERKKETE RKSEGGKEKE RLRDRDRERD RDKGKDRDRR RVKNGEHSWD LDREKNREHD
KPEKKSASSG EMSKKLSDGT FKDSKAETET EISTRASKSL TTKTSKRRSK NSVEGRKEDN
ISAKSLDSIV SGINNEPNQE TTTSEIGTKE ANINSTSISD DNSASLRCEN IQPNPTEKQK
GDSTSDAEGD AGPAGQDKSE VPETPEIPNE LSSNIRRIPR PGSARPAPPR VKRQDSMEAL
QMDRSGSGKT VSNVITESHN SDNEEDDQFV VEAAPQLSEM SEIEMVTAVE LEEEEKHGGL
VKKILETKKD YEKLQQSPKP GEKERSLFES AWKKEKDIVS KEIEKLRTSI QTLCKSALPL
GKIMDYIQED VDAMQNELQM WHSENRQHAE ALQQEQRITD CAVEPLKAEL AELEQLIKDQ
QDKICAVKAN ILKNEEKIQK MVYSINLTSR R
