DC2I1_HUMAN
ID DC2I1_HUMAN Reviewed; 1066 AA.
AC Q8WVS4; Q9NW58;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Cytoplasmic dynein 2 intermediate chain 1;
DE AltName: Full=Dynein 2 intermediate chain 1;
DE AltName: Full=WD repeat-containing protein 60;
GN Name=DYNC2I1 {ECO:0000312|HGNC:HGNC:21862}; Synonyms=WDR60;
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 GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 710-1066.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP 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 [6]
RP IDENTIFICATION IN THE CYTOPLASMIC DYNEIN 2 COMPLEX, SUBCELLULAR LOCATION,
RP AND FUNCTION.
RX PubMed=25205765; DOI=10.1242/jcs.159038;
RA Asante D., Stevenson N.L., Stephens D.J.;
RT "Subunit composition of the human cytoplasmic dynein-2 complex.";
RL J. Cell Sci. 127:4774-4787(2014).
RN [7]
RP VARIANT SRTD8 642-ARG--LYS-1066 DEL.
RX PubMed=25492405; DOI=10.1111/cge.12550;
RA McInerney-Leo A.M., Harris J.E., Leo P.J., Marshall M.S., Gardiner B.,
RA Kinning E., Leong H.Y., McKenzie F., Ong W.P., Vodopiutz J., Wicking C.,
RA Brown M.A., Zankl A., Duncan E.L.;
RT "Whole exome sequencing is an efficient, sensitive and specific method for
RT determining the genetic cause of short-rib thoracic dystrophies.";
RL Clin. Genet. 88:550-557(2015).
RN [8]
RP INTERACTION WITH DYNLT2B.
RX PubMed=26044572; DOI=10.1038/ncomms8074;
RG UK10K;
RA Schmidts M., Hou Y., Cortes C.R., Mans D.A., Huber C., Boldt K., Patel M.,
RA van Reeuwijk J., Plaza J.M., van Beersum S.E., Yap Z.M., Letteboer S.J.,
RA Taylor S.P., Herridge W., Johnson C.A., Scambler P.J., Ueffing M.,
RA Kayserili H., Krakow D., King S.M., Beales P.L., Al-Gazali L., Wicking C.,
RA Cormier-Daire V., Roepman R., Mitchison H.M., Witman G.B.;
RT "TCTEX1D2 mutations underlie Jeune asphyxiating thoracic dystrophy with
RT impaired retrograde intraflagellar transport.";
RL Nat. Commun. 6:7074-7074(2015).
RN [9]
RP ERRATUM OF PUBMED:26044572.
RX PubMed=27021811; DOI=10.1038/ncomms11270;
RG UK10K;
RA Schmidts M., Hou Y., Cortes C.R., Mans D.A., Huber C., Boldt K., Patel M.,
RA van Reeuwijk J., Plaza J.M., van Beersum S.E., Yap Z.M., Letteboer S.J.,
RA Taylor S.P., Herridge W., Johnson C.A., Scambler P.J., Ueffing M.,
RA Kayserili H., Krakow D., King S.M., Beales P.L., Al-Gazali L., Wicking C.,
RA Cormier-Daire V., Roepman R., Mitchison H.M., Witman G.B.;
RL Nat. Commun. 7:11270-11270(2016).
RN [10]
RP VARIANTS SRTD8 631-GLN--LYS-1066 DEL AND MET-749, FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23910462; DOI=10.1016/j.ajhg.2013.06.022;
RA McInerney-Leo A.M., Schmidts M., Cortes C.R., Leo P.J., Gener B.,
RA Courtney A.D., Gardiner B., Harris J.A., Lu Y., Marshall M., Scambler P.J.,
RA Beales P.L., Brown M.A., Zankl A., Mitchison H.M., Duncan E.L., Wicking C.;
RT "Short-rib polydactyly and Jeune syndromes are caused by mutations in
RT WDR60.";
RL Am. J. Hum. Genet. 93:515-523(2013).
RN [11]
RP SUBUNIT, FUNCTION, AND INTERACTION WITH DYNC2I2.
RX PubMed=29742051; DOI=10.1091/mbc.e18-03-0173;
RA Hamada Y., Tsurumi Y., Nozaki S., Katoh Y., Nakayama K.;
RT "Interaction of WDR60 intermediate chain with TCTEX1D2 light chain of the
RT dynein-2 complex is crucial for ciliary protein trafficking.";
RL Mol. Biol. Cell 29:1628-1639(2018).
RN [12]
RP FUNCTION, INTERACTION WITH DYNC2I2, AND CHARACTERIZATION OF VARIANTS SRTD8
RP 631-GLN--LYS-1066 DEL AND MET-749.
RX PubMed=30320547; DOI=10.7554/elife.39655;
RA Vuolo L., Stevenson N.L., Heesom K.J., Stephens D.J.;
RT "Dynein-2 intermediate chains play crucial but distinct roles in primary
RT cilia formation and function.";
RL Elife 7:0-0(2018).
RN [13]
RP FUNCTION.
RX PubMed=30649997; DOI=10.1091/mbc.e18-10-0678;
RA Tsurumi Y., Hamada Y., Katoh Y., Nakayama K.;
RT "Interactions of the dynein-2 intermediate chain WDR34 with the light
RT chains are required for ciliary retrograde protein trafficking.";
RL Mol. Biol. Cell 30:658-670(2019).
RN [14] {ECO:0007744|PDB:6RLB, ECO:0007744|PDB:6SC2}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) OF THE CYTOPLASMIC DYNEIN
RP 2 COMPLEX, AND SUBUNIT.
RX PubMed=31451806; DOI=10.1038/s41594-019-0286-y;
RA Toropova K., Zalyte R., Mukhopadhyay A.G., Mladenov M., Carter A.P.,
RA Roberts A.J.;
RT "Structure of the dynein-2 complex and its assembly with intraflagellar
RT transport trains.";
RL Nat. Struct. Mol. Biol. 26:823-829(2019).
CC -!- FUNCTION: Acts as one of several non-catalytic accessory components of
CC the cytoplasmic dynein 2 complex (dynein-2 complex), a motor protein
CC complex that drives the movement of cargos along microtubules within
CC cilia and flagella in concert with the intraflagellar transport (IFT)
CC system (PubMed:23910462, PubMed:25205765, PubMed:31451806,
CC PubMed:29742051). DYNC2I1 plays a major role in retrograde ciliary
CC protein trafficking in cilia and flagella (PubMed:29742051,
CC PubMed:30320547, PubMed:30649997). Requires also to maintain a
CC functional transition zone (PubMed:30320547).
CC {ECO:0000269|PubMed:23910462, ECO:0000269|PubMed:25205765,
CC ECO:0000269|PubMed:29742051, ECO:0000269|PubMed:30320547,
CC ECO:0000269|PubMed:30649997, ECO:0000269|PubMed:31451806}.
CC -!- SUBUNIT: Intermediate chain of the cytoplasmic dynein complex 2, a
CC multisubunit complex, composed at least of eleven different proteins
CC (PubMed:31451806, PubMed:25205765). The cytoplasmic dynein 2 complex
CC consists of two catalytic heavy chains (HCs) and a number of non-
CC catalytic subunits presented by intermediate chains (ICs), light
CC intermediate chains (LICs) and light chains (LCs). Among them, a heavy
CC chain (DYNC2H1), two intermediate chains (DYNC2I2 and DYNC2I1), a light
CC intermediate chain (DYNC2LI1), and a light chain (DYNLT2B) are unique
CC to the cytoplasmic dynein complex 2, but a subset of the light chains
CC are also shared by dynein-1 and dynein-2 complexes (PubMed:25205765,
CC PubMed:31451806). Interacts with DYNC2I2; their C-terminal domains each
CC bind a copy of the heavy chain, and their extended N-terminal regions
CC are held together by an array of light chain dimers (PubMed:29742051,
CC PubMed:31451806, PubMed:30320547). Interacts with DYNLT2B
CC (PubMed:26044572). Interacts (via the N-terminal half) with DYNLT2B-
CC DYNLT1 dimer or with DYNLT2B-DYNLT3 dimer; this interaction is crucial
CC for retrograde trafficking of ciliary proteins (PubMed:29742051).
CC {ECO:0000269|PubMed:25205765, ECO:0000269|PubMed:26044572,
CC ECO:0000269|PubMed:29742051, ECO:0000269|PubMed:30320547,
CC ECO:0000269|PubMed:31451806}.
CC -!- INTERACTION:
CC Q8WVS4; Q9Y266: NUDC; NbExp=3; IntAct=EBI-2556085, EBI-357298;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:23910462}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:25205765}.
CC Note=Located at the base of the primary cilium in serum-starved
CC fibroblasts. {ECO:0000269|PubMed:23910462}.
CC -!- TISSUE SPECIFICITY: Expressed in chondrocytes (at protein level).
CC {ECO:0000269|PubMed:23910462}.
CC -!- DISEASE: Short-rib thoracic dysplasia 8 with or without polydactyly
CC (SRTD8) [MIM:615503]: A form of short-rib thoracic dysplasia, a group
CC of autosomal recessive ciliopathies that are characterized by a
CC constricted thoracic cage, short ribs, shortened tubular bones, and a
CC 'trident' appearance of the acetabular roof. Polydactyly is variably
CC present. Non-skeletal involvement can include cleft lip/palate as well
CC as anomalies of major organs such as the brain, eye, heart, kidneys,
CC liver, pancreas, intestines, and genitalia. Some forms of the disease
CC are lethal in the neonatal period due to respiratory insufficiency
CC secondary to a severely restricted thoracic cage, whereas others are
CC compatible with life. Disease spectrum encompasses Ellis-van Creveld
CC syndrome, asphyxiating thoracic dystrophy (Jeune syndrome), Mainzer-
CC Saldino syndrome, and short rib-polydactyly syndrome.
CC {ECO:0000269|PubMed:23910462, ECO:0000269|PubMed:25492405,
CC ECO:0000269|PubMed:30320547}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. Fibroblasts from affected
CC individuals exhibit a defect in ciliogenesis and aberrant accumulation
CC of the GLI2 transcription factor at the centrosome or basal body in the
CC absence of an obvious axoneme.
CC -!- SIMILARITY: Belongs to the dynein light intermediate chain family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91528.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC004863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014491; AAH14491.2; -; mRNA.
DR EMBL; AK001162; BAA91528.1; ALT_INIT; mRNA.
DR CCDS; CCDS47757.1; -.
DR RefSeq; NP_060521.4; NM_018051.4.
DR PDB; 6RLB; EM; 4.50 A; C=1-1066.
DR PDB; 6SC2; EM; 3.90 A; C=1-1066.
DR PDBsum; 6RLB; -.
DR PDBsum; 6SC2; -.
DR AlphaFoldDB; Q8WVS4; -.
DR SMR; Q8WVS4; -.
DR BioGRID; 120422; 42.
DR CORUM; Q8WVS4; -.
DR IntAct; Q8WVS4; 28.
DR MINT; Q8WVS4; -.
DR STRING; 9606.ENSP00000384290; -.
DR iPTMnet; Q8WVS4; -.
DR PhosphoSitePlus; Q8WVS4; -.
DR BioMuta; WDR60; -.
DR DMDM; 296453073; -.
DR EPD; Q8WVS4; -.
DR jPOST; Q8WVS4; -.
DR MassIVE; Q8WVS4; -.
DR MaxQB; Q8WVS4; -.
DR PaxDb; Q8WVS4; -.
DR PeptideAtlas; Q8WVS4; -.
DR PRIDE; Q8WVS4; -.
DR ProteomicsDB; 74818; -.
DR Antibodypedia; 10739; 44 antibodies from 11 providers.
DR DNASU; 55112; -.
DR Ensembl; ENST00000407559.8; ENSP00000384290.3; ENSG00000126870.16.
DR GeneID; 55112; -.
DR KEGG; hsa:55112; -.
DR MANE-Select; ENST00000407559.8; ENSP00000384290.3; NM_018051.5; NP_060521.4.
DR UCSC; uc003woe.5; human.
DR CTD; 55112; -.
DR DisGeNET; 55112; -.
DR GeneCards; DYNC2I1; -.
DR HGNC; HGNC:21862; DYNC2I1.
DR HPA; ENSG00000126870; Low tissue specificity.
DR MalaCards; DYNC2I1; -.
DR MIM; 615462; gene.
DR MIM; 615503; phenotype.
DR neXtProt; NX_Q8WVS4; -.
DR OpenTargets; ENSG00000126870; -.
DR Orphanet; 474; Jeune syndrome.
DR Orphanet; 93271; Short rib-polydactyly syndrome, Verma-Naumoff type.
DR VEuPathDB; HostDB:ENSG00000126870; -.
DR eggNOG; KOG1587; Eukaryota.
DR GeneTree; ENSGT00390000013743; -.
DR HOGENOM; CLU_010610_0_0_1; -.
DR InParanoid; Q8WVS4; -.
DR OMA; ILNMWVV; -.
DR OrthoDB; 1158787at2759; -.
DR PhylomeDB; Q8WVS4; -.
DR TreeFam; TF329081; -.
DR PathwayCommons; Q8WVS4; -.
DR Reactome; R-HSA-5620924; Intraflagellar transport.
DR SignaLink; Q8WVS4; -.
DR BioGRID-ORCS; 55112; 7 hits in 1077 CRISPR screens.
DR ChiTaRS; WDR60; human.
DR GenomeRNAi; 55112; -.
DR Pharos; Q8WVS4; Tbio.
DR PRO; PR:Q8WVS4; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q8WVS4; protein.
DR Bgee; ENSG00000126870; Expressed in sural nerve and 180 other tissues.
DR ExpressionAtlas; Q8WVS4; baseline and differential.
DR Genevisible; Q8WVS4; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0097546; C:ciliary base; IDA:GO_Central.
DR GO; GO:0097014; C:ciliary plasm; IBA:GO_Central.
DR GO; GO:0097542; C:ciliary tip; TAS:Reactome.
DR GO; GO:0005929; C:cilium; TAS:Reactome.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0000242; C:pericentriolar material; IDA:GO_Central.
DR GO; GO:0045504; F:dynein heavy chain binding; IBA:GO_Central.
DR GO; GO:0045503; F:dynein light chain binding; IPI:GO_Central.
DR GO; GO:0060271; P:cilium assembly; IMP:GO_Central.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:GO_Central.
DR GO; GO:0035721; P:intraciliary retrograde transport; IDA:UniProtKB.
DR GO; GO:0042073; P:intraciliary transport; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR042505; DYNC2I1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR16022; PTHR16022; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Ciliopathy; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Disease variant;
KW Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1066
FT /note="Cytoplasmic dynein 2 intermediate chain 1"
FT /id="PRO_0000242142"
FT REPEAT 694..734
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 775..821
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 907..947
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 952..992
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REGION 22..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..552
FT /note="Binding to the DYNLT2B-DYNLT1/DYNLT3 dimer"
FT /evidence="ECO:0000269|PubMed:29742051"
FT COMPBIAS 22..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..396
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 91
FT /note="E -> G (in dbSNP:rs17837851)"
FT /id="VAR_026841"
FT VARIANT 273
FT /note="Q -> R (in dbSNP:rs2788478)"
FT /id="VAR_026842"
FT VARIANT 631..1066
FT /note="Missing (in SRTD8; Reduces interaction with IFT
FT proteins)"
FT /evidence="ECO:0000269|PubMed:23910462,
FT ECO:0000269|PubMed:30320547"
FT /id="VAR_083839"
FT VARIANT 642..1066
FT /note="Missing (in SRTD8)"
FT /evidence="ECO:0000269|PubMed:25492405"
FT /id="VAR_079178"
FT VARIANT 749
FT /note="T -> M (in SRTD8; does not affect interaction with
FT DYNC2I2; dbSNP:rs587777065)"
FT /evidence="ECO:0000269|PubMed:23910462,
FT ECO:0000269|PubMed:30320547"
FT /id="VAR_070197"
FT CONFLICT 225
FT /note="N -> K (in Ref. 2; AAH14491)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="S -> F (in Ref. 2; AAH14491)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1066 AA; 122571 MW; A6B4A0C3DC4CD2C2 CRC64;
MEPGKRRTKD DTWKADDLRK HLWAIQSGGS KEERKHREKK LRKESEMDLP EHKEPRCRDP
DQDARSRDRV AEVHTAKESP RGERDRDRQR ERRRDAKDRE KEKLKEKHRE AEKSHSRGKD
REKEKDRRAR KEELRQTVAH HNLLGQETRD RQLLERAERK GRSVSKVRSE EKDEDSERGD
EDRERRYRER KLQYGDSKDN PLKYWLYKEE GERRHRKPRE PDRDNKHREK SSTREKREKY
SKEKSNSFSD KGEERHKEKR HKEGFHFDDE RHQSNVDRKE KSAKDEPRKR ESQNGEHRNR
GASSKRDGTS SQHAENLVRN HGKDKDSRRK HGHEEGSSVW WKLDQRPGGE ETVEIEKEET
DLENARADAY TASCEDDFED YEDDFEVCDG DDDESSNEPE SREKLEELPL AQKKEIQEIQ
RAINAENERI GELSLKLFQK RGRTEFEKEP RTDTNSSPSR ASVCGIFVDF ASASHRQKSR
TQALKQKMRS TKLLRLIDLD FSFTFSLLDL PPVNEYDMYI RNFGKKNTKQ AYVQCNEDNV
ERDIQTEEIE TREVWTQHPG ESTVVSGGSE QRDTSDAVVM PKIDTPRLCS FLRAACQVMA
VLLEEDRLAA EPSWNLRAQD RALYFSDSSS QLNTSLPFLQ NRKVSSLHTS RVQRQMVVSV
HDLPEKSFVP LLDSKYVLCV WDIWQPSGPQ KVLICESQVT CCCLSPLKAF LLFAGTAHGS
VVVWDLREDS RLHYSVTLSD GFWTFRTATF STDGILTSVN HRSPLQAVEP ISTSVHKKQS
FVLSPFSTQE EMSGLSFHIA SLDESGVLNV WVVVELPKAD IAGSISDLGL MPGGRVKLVH
SALIQLGDSL SHKGNEFWGT TQTLNVKFLP SDPNHFIIGT DMGLISHGTR QDLRVAPKLF
KPQQHGIRPV KVNVIDFSPF GEPIFLAGCS DGSIRLHQLS SAFPLLQWDS STDSHAVTGL
QWSPTRPAVF LVQDDTSNIY IWDLLQSDLG PVAKQQVSPN RLVAMAAVGE PEKAGGSFLA
LVLARASGSI DIQHLKRRWA APEVDECNRL RLLLQEALWP EGKLHK
