DCI2A_DANRE
ID DCI2A_DANRE Reviewed; 626 AA.
AC E7F6H7;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Dynein, cytoplasmic 1, intermediate chain 2a {ECO:0000312|ZFIN:ZDB-GENE-060929-1086};
GN Name=dync1i2a {ECO:0000312|ZFIN:ZDB-GENE-060929-1086};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31079899; DOI=10.1016/j.ajhg.2019.04.002;
RA Ansar M., Ullah F., Paracha S.A., Adams D.J., Lai A., Pais L.,
RA Iwaszkiewicz J., Millan F., Sarwar M.T., Agha Z., Shah S.F., Qaisar A.A.,
RA Falconnet E., Zoete V., Ranza E., Makrythanasis P., Santoni F.A., Ahmed J.,
RA Katsanis N., Walsh C., Davis E.E., Antonarakis S.E.;
RT "Bi-allelic variants in DYNC1I2 cause syndromic microcephaly with
RT intellectual disability, cerebral malformations, and dysmorphic facial
RT features.";
RL Am. J. Hum. Genet. 104:1073-1087(2019).
CC -!- FUNCTION: Acts as one of several non-catalytic accessory components of
CC the cytoplasmic dynein 1 complex that are thought to be involved in
CC linking dynein to cargos and to adapter proteins that regulate dynein
CC function. Cytoplasmic dynein 1 acts as a motor for the intracellular
CC retrograde motility of vesicles and organelles along microtubules (By
CC similarity). Plays a role in the development of anterior brain and
CC cartilaginous structures (PubMed:31079899).
CC {ECO:0000250|UniProtKB:Q13409, ECO:0000269|PubMed:31079899}.
CC -!- SUBUNIT: Homodimer. The cytoplasmic dynein 1 complex consists of two
CC catalytic heavy chains (HCs) and a number of non-catalytic subunits
CC presented by intermediate chains (ICs), light intermediate chains
CC (LICs) and light chains (LCs); the composition seems to vary in respect
CC to the IC, LIC and LC composition. The heavy chain homodimer serves as
CC a scaffold for the probable homodimeric assembly of the respective non-
CC catalytic subunits. The ICs and LICs bind directly to the HC dimer and
CC the LCs assemble on the IC dimer. {ECO:0000250|UniProtKB:Q13409}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O88487}. Cytoplasm
CC {ECO:0000250|UniProtKB:O88487}.
CC -!- DISRUPTION PHENOTYPE: Morphant embryos display defective craniofacial
CC patterning, microcephaly, a marked disorganization of axonal patterning
CC in the head, reduced number of axon tracts crossing the dorsal midline,
CC and increased cell death. {ECO:0000269|PubMed:31079899}.
CC -!- SIMILARITY: Belongs to the dynein intermediate chain family.
CC {ECO:0000305}.
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DR EMBL; CU222541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU929261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FP245477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FQ377636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E7F6H7; -.
DR SMR; E7F6H7; -.
DR STRING; 7955.ENSDARP00000123958; -.
DR PeptideAtlas; E7F6H7; -.
DR Ensembl; ENSDART00000007756; ENSDARP00000009095; ENSDARG00000078386.
DR ZFIN; ZDB-GENE-060929-1086; dync1i2a.
DR GeneTree; ENSGT00940000155442; -.
DR HOGENOM; CLU_012999_1_1_1; -.
DR InParanoid; E7F6H7; -.
DR OrthoDB; 1453532at2759; -.
DR TreeFam; TF300553; -.
DR PRO; PR:E7F6H7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 9.
DR Bgee; ENSDARG00000078386; Expressed in intestine and 23 other tissues.
DR ExpressionAtlas; E7F6H7; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IBA:GO_Central.
DR GO; GO:0045504; F:dynein heavy chain binding; IBA:GO_Central.
DR GO; GO:0045503; F:dynein light chain binding; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:ZFIN.
DR GO; GO:0010970; P:transport along microtubule; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR025956; DYNC1I1/DYNC1I2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF11540; Dynein_IC2; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; Reference proteome; Repeat; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT CHAIN 2..626
FT /note="Dynein, cytoplasmic 1, intermediate chain 2a"
FT /id="PRO_0000448836"
FT REPEAT 265..314
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 318..358
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 367..408
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 417..457
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 462..507
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 510..550
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 556..595
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 20..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 626 AA; 70172 MW; A92D9E1B34376AE2 CRC64;
MSDKSELKAE LERKKQRLAQ IREEKKRKEE ERKKKEAELK KDAVPLQDDS DLEKKRREAD
ALLQSMGITS DVSAAPAPMS PTAKSVGSPS EAGSQDSGDG TTGPRTLHWD CDPSTVLLHS
ELGRGPLKLA MTKMTHVDFP PKEVVSYTKE TQTPTMTEQK DEEDEEEETP AAQPEAETEK
EKPEEKQVEE ALPHELTEEE KLQILHSEEF MDFFDHSTRI VERALSEHVD VFFDYSGRDM
EEKEGEMQAG TKLSLNRKFV DDRWSKQRVV TCLDWSPQYP ELLVASYNNN EEAPHEPDGV
ALVWNMKYKK ATPEYVFHCQ SAVMSAAFAK FHPNLVVGGT YSGQIVLWDN RSNRRTPVQR
TPLSAAAHTH PVYCVNVVGT QNAHNLISIS TDGKMCSWSL DMLSQPQDSM ELVFKQSKSV
AVTSMSFPLG DVNNFVVGSE DGSVYTASRH GSRAGISEMF EGHHGPITGI HCHTAAGPVD
FSHLFLTASF DWTVKLWSNK NNKPLYSFED NSDYVYDVMW SPVHPALFAC VDGLGRVDLW
NLNNDTEVPT ASVAVDGSPA LNRLRWSQSG REIAVGDSEG QIHIYDVGEQ IAVPRNDEWT
RFVRTLVEIN ENRDDAEELA AQRLAA
