ID A0A673VS49_SURSU Unreviewed; 638 AA.
AC A0A673VS49;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 18-JUN-2025, entry version 23.
DE RecName: Full=Cytoplasmic dynein 1 intermediate chain 2 {ECO:0000256|ARBA:ARBA00040292};
DE AltName: Full=Cytoplasmic dynein intermediate chain 2 {ECO:0000256|ARBA:ARBA00042023};
DE AltName: Full=Dynein intermediate chain 2, cytosolic {ECO:0000256|ARBA:ARBA00042966};
OS Suricata suricatta (Meerkat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Herpestidae; Suricata.
OX NCBI_TaxID=37032 {ECO:0000313|Ensembl:ENSSSUP00005036757.1, ECO:0000313|Proteomes:UP000472268};
RN [1] {ECO:0000313|Ensembl:ENSSSUP00005036757.1, ECO:0000313|Proteomes:UP000472268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dudchenko O., Lieberman Aiden E., Tung J., Barreiro L.B.,
RA Clutton-Brock T.H.;
RT "A Chromosome-scale Meerkat (S. suricatta) Genome Assembly.";
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSUP00005036757.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
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. The
CC intermediate chains mediate the binding of dynein to dynactin via its
CC 150 kDa component (p150-glued) DCTN1. Involved in membrane-transport,
CC such as Golgi apparatus, late endosomes and lysosomes.
CC {ECO:0000256|ARBA:ARBA00045429}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the dynein intermediate chain family.
CC {ECO:0000256|ARBA:ARBA00011059}.
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DR AlphaFoldDB; A0A673VS49; -.
DR Ensembl; ENSSSUT00005041858.1; ENSSSUP00005036757.1; ENSSSUG00005023507.1.
DR OMA; MHDRPEY; -.
DR Proteomes; UP000472268; Chromosome 3.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IEA:InterPro.
DR GO; GO:0045504; F:dynein heavy chain binding; IEA:TreeGrafter.
DR GO; GO:0045503; F:dynein light chain binding; IEA:TreeGrafter.
DR GO; GO:0010970; P:transport along microtubule; IEA:TreeGrafter.
DR FunFam; 2.130.10.10:FF:000095; Cytoplasmic dynein 1 intermediate chain 2; 1.
DR FunFam; 2.130.10.10:FF:000026; cytoplasmic dynein 1 intermediate chain 2 isoform X2; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR025956; DYNC1I1/DYNC1I2.
DR InterPro; IPR050687; Dynein_IC.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR12442:SF37; CYTOPLASMIC DYNEIN 1 INTERMEDIATE CHAIN 2; 1.
DR PANTHER; PTHR12442; DYNEIN INTERMEDIATE CHAIN; 1.
DR Pfam; PF11540; Dynein_IC2; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Dynein {ECO:0000256|ARBA:ARBA00023017};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000472268};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574}.
FT REGION 1..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..13
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..97
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 638 AA; 71485 MW; DA424810A01CDA5C CRC64;
MSDKSELKAE LERKKQRLAQ IREEKKRKEE ERKKKETDQK KEAVAPVQEE SDLEKKRREA
EALLQSMGLT PESPIVFSEY WVPPPMSPSS KSVSTPSEAG SQDSGDGAVG SRTLHWDTDP
SVLQLHSDSD LGRGPIKLGM AKITQVDFPP REIVTYTKET QTPVVAQPKE DEEEEDDVVT
PKPPIEPEEE KTLKKDEEND SKAPPHELTE EEKQQILHSE EFLSFFDHST RIVERALSEQ
INIFFDYSGR DLEDKEGEIQ AGAKLSLNRQ FFDERWSKHR VVSCLDWSSQ YPELLVASYN
NNEDAPHEPD GVALVWNMKY KKTTPEYVFH CQSAVMSATF AKFHPNLVVG GTYSGQIVLW
DNRSNKRTPV QRTPLSAAAH THPVYCVNVV GTQNAHNLIS ISTDGKICSW SLDMLSHPQD
SMELVHKQSK AVAVTSMSFP VGDVNNFVVG SEEGSVYTAC RHGSKAGISE MFEGHQGPIT
GIHCHAAVGA VDFSHLFVTS SFDWTVKLWT TKNNKPLYSF EDNSDYVYDV MWSPTHPALF
ACVDGMGRLD LWNLNNDTEV PTASISVEGN PALNRVRWTH SGREIAVGDS EGQIVIYDVG
EQIAVPRNDE WARFGRTLAE INANRADAEE EAATRIPA
//
