DC1I2_PONAB
ID DC1I2_PONAB Reviewed; 638 AA.
AC Q5NVM2; Q5R985; Q5RDM7;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Cytoplasmic dynein 1 intermediate chain 2;
DE AltName: Full=Cytoplasmic dynein intermediate chain 2;
DE AltName: Full=Dynein intermediate chain 2, cytosolic;
DE Short=DH IC-2;
GN Name=DYNC1I2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q62871}.
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. Interacts with DYNLT3. Interacts with
CC DYNLT1. Interacts (dephosphorylated at Ser-90) with DCTN1 (By
CC similarity). Interacts with BICD2. Interacts with SPEF2 (By
CC similarity). {ECO:0000250|UniProtKB:O88487,
CC ECO:0000250|UniProtKB:Q62871}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O88487}. Cytoplasm
CC {ECO:0000250|UniProtKB:O88487}. Note=Detected in the cytoplasm of
CC pachytene spermatocytes. Localizes to the manchette in elongating
CC spermatids. {ECO:0000250|UniProtKB:O88487}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5NVM2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5NVM2-2; Sequence=VSP_023012;
CC Name=3;
CC IsoId=Q5NVM2-3; Sequence=VSP_023013;
CC -!- PTM: The phosphorylation status of Ser-90 appears to be involved in
CC dynactin-dependent target binding. {ECO:0000250|UniProtKB:Q62871}.
CC -!- PTM: Pyrophosphorylation by 5-diphosphoinositol pentakisphosphate (5-
CC IP7) promotes interaction with DCTN1. Serine pyrophosphorylation is
CC achieved by Mg(2+)-dependent, but enzyme independent transfer of a
CC beta-phosphate from a inositol pyrophosphate to a pre-phosphorylated
CC serine residue. {ECO:0000250|UniProtKB:O88487}.
CC -!- SIMILARITY: Belongs to the dynein intermediate chain family.
CC {ECO:0000305}.
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DR EMBL; CR857877; CAH90130.1; -; mRNA.
DR EMBL; CR859506; CAH91675.1; -; mRNA.
DR EMBL; CR926000; CAI29641.1; -; mRNA.
DR RefSeq; NP_001127088.1; NM_001133616.1. [Q5NVM2-1]
DR RefSeq; NP_001128826.1; NM_001135354.1.
DR AlphaFoldDB; Q5NVM2; -.
DR SMR; Q5NVM2; -.
DR STRING; 9601.ENSPPYP00000014432; -.
DR Ensembl; ENSPPYT00000015018; ENSPPYP00000014432; ENSPPYG00000012930. [Q5NVM2-2]
DR Ensembl; ENSPPYT00000035165; ENSPPYP00000028264; ENSPPYG00000012930. [Q5NVM2-1]
DR GeneID; 100174119; -.
DR KEGG; pon:100174119; -.
DR CTD; 1781; -.
DR eggNOG; KOG1587; Eukaryota.
DR GeneTree; ENSGT00940000155442; -.
DR HOGENOM; CLU_012999_1_1_1; -.
DR InParanoid; Q5NVM2; -.
DR OMA; EEGSIYP; -.
DR TreeFam; TF300553; -.
DR Proteomes; UP000001595; Chromosome 2B.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IEA:InterPro.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
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; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton; Dynein;
KW Microtubule; Motor protein; Phosphoprotein; Reference proteome; Repeat;
KW Transport; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT CHAIN 2..638
FT /note="Cytoplasmic dynein 1 intermediate chain 2"
FT /id="PRO_0000277463"
FT REPEAT 277..326
FT /note="WD 1"
FT REPEAT 330..370
FT /note="WD 2"
FT REPEAT 379..420
FT /note="WD 3"
FT REPEAT 429..469
FT /note="WD 4"
FT REPEAT 474..519
FT /note="WD 5"
FT REPEAT 522..562
FT /note="WD 6"
FT REPEAT 568..607
FT /note="WD 7"
FT REGION 1..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT MOD_RES 51
FT /note="Diphosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88487"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62871"
FT MOD_RES 95
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT VAR_SEQ 77..82
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_023012"
FT VAR_SEQ 602
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_023013"
FT CONFLICT 41
FT /note="K -> E (in Ref. 1; CAH90130)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="N -> S (in Ref. 1; CAH91675)"
FT /evidence="ECO:0000305"
FT CONFLICT 580
FT /note="H -> Y (in Ref. 1; CAH90130)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 638 AA; 71457 MW; 2F868EC9556C47F2 CRC64;
MSDKSELKAE LERKKQRLAQ IREEKKRKEE ERKKKETDQK KEAVAPVQEE SDLEKKRREA
EALLQSMGLT PESPIVFSEY WVPPPMSPSS KSVSTPSEAG SQDSGDGAVG SRTLHWDTDP
SVLQLHSDSD LGRGPIKLGM AKITQVDFPP REIVTYTKET QTPVMAQPKE DEEEDDDVVA
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 EDNADYVYDV MWSPTHPALF
ACVDGMGRLD LWNLNNDTEV PTASISVEGN PALNRVRWTH SGREIAVGDS EGQIVIYDVG
EQIAVPRNDE WARFGRTLAE INANRADAEE EAATRIPA
