DCTN2_RAT
ID DCTN2_RAT Reviewed; 402 AA.
AC Q6AYH5;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Dynactin subunit 2;
GN Name=Dctn2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP PROTEIN SEQUENCE OF 269-283; 320-333 AND 381-396, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-199, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Modulates cytoplasmic dynein binding to an organelle, and
CC plays a role in prometaphase chromosome alignment and spindle
CC organization during mitosis. Involved in anchoring microtubules to
CC centrosomes. May play a role in synapse formation during brain
CC development (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Subunit of dynactin, a multiprotein complex associated with
CC dynein. Interacts with BICD2, CEP135, DYNAP, ECPAS and MAPRE1.
CC {ECO:0000250|UniProtKB:Q13561, ECO:0000250|UniProtKB:Q99KJ8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dynactin subunit 2 family. {ECO:0000305}.
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DR EMBL; BC079042; AAH79042.1; -; mRNA.
DR RefSeq; NP_001004239.1; NM_001004239.1.
DR AlphaFoldDB; Q6AYH5; -.
DR BioGRID; 256357; 8.
DR IntAct; Q6AYH5; 5.
DR MINT; Q6AYH5; -.
DR STRING; 10116.ENSRNOP00000008120; -.
DR iPTMnet; Q6AYH5; -.
DR PhosphoSitePlus; Q6AYH5; -.
DR jPOST; Q6AYH5; -.
DR PaxDb; Q6AYH5; -.
DR PRIDE; Q6AYH5; -.
DR Ensembl; ENSRNOT00000008120; ENSRNOP00000008120; ENSRNOG00000025481.
DR GeneID; 299850; -.
DR KEGG; rno:299850; -.
DR UCSC; RGD:1303182; rat.
DR CTD; 10540; -.
DR RGD; 1303182; Dctn2.
DR eggNOG; KOG3958; Eukaryota.
DR GeneTree; ENSGT00390000003427; -.
DR HOGENOM; CLU_049964_1_0_1; -.
DR InParanoid; Q6AYH5; -.
DR OrthoDB; 951183at2759; -.
DR PhylomeDB; Q6AYH5; -.
DR TreeFam; TF105247; -.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-RNO-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-8854518; AURKA Activation by TPX2.
DR PRO; PR:Q6AYH5; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000025481; Expressed in testis and 19 other tissues.
DR ExpressionAtlas; Q6AYH5; baseline and differential.
DR Genevisible; Q6AYH5; RN.
DR GO; GO:0005813; C:centrosome; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; TAS:RGD.
DR GO; GO:0005869; C:dynactin complex; IDA:RGD.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR GO; GO:0030426; C:growth cone; ISO:RGD.
DR GO; GO:0000776; C:kinetochore; IDA:RGD.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0030507; F:spectrin binding; ISO:RGD.
DR GO; GO:0032402; P:melanosome transport; ISO:RGD.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; IDA:RGD.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISO:RGD.
DR GO; GO:0007052; P:mitotic spindle organization; IDA:RGD.
DR GO; GO:0071539; P:protein localization to centrosome; ISO:RGD.
DR InterPro; IPR028133; Dynamitin.
DR PANTHER; PTHR15346; PTHR15346; 1.
DR Pfam; PF04912; Dynamitin; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Dynein; Membrane; Microtubule; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13561"
FT CHAIN 2..402
FT /note="Dynactin subunit 2"
FT /id="PRO_0000288766"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 100..130
FT /evidence="ECO:0000255"
FT COILED 215..247
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q13561"
FT MOD_RES 6
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q13561"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13561"
FT MOD_RES 86
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99KJ8"
FT MOD_RES 134
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13561"
FT MOD_RES 199
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99KJ8"
SQ SEQUENCE 402 AA; 44148 MW; 550335535A4FB052 CRC64;
MADPKYADLP GIARNEPDVY ETSDLPEDDQ AEFDAEELSS TSVEHIIVNP NAAYDKFKDK
RVGTKGLDFS DRIGKTKRTG YESGDYEMLG EGLGVKETPQ QKYQRLLHEV QELTTEVEKI
KTTVKESATE EKLTPVVLAK QLAALKQQLV ASHLEKLLGP DAAINLADPD GALAKRLLLQ
LEATKSSKGS SGGKSTGGTP PDSSLVTYEL HSRPEQDKFS QAAKVAELEK RLTELEATVR
CDQDAQNPLS AGLQGACLME TVELLQAKVN ALDLAVLDQV EARLQSVLGK VNEIAKHKAS
VEDADTQNKV HQLYETIQRW SPVASTLPEL VQRLVTIKQL HEQAMQFGQL LTHLDTTQQM
MASSLKDNTA LLTQVQTTMR ENLATVEGNF ASIDARMKKL GK
