ID   DCTN2_BOVIN             Reviewed;         403 AA.
AC   Q3ZCF0;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Dynactin subunit 2;
GN   Name=DCTN2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; BC102441; AAI02442.1; -; mRNA.
DR   RefSeq; NP_001029730.1; NM_001034558.1.
DR   AlphaFoldDB; Q3ZCF0; -.
DR   BioGRID; 183812; 1.
DR   CORUM; Q3ZCF0; -.
DR   STRING; 9913.ENSBTAP00000014053; -.
DR   PaxDb; Q3ZCF0; -.
DR   PeptideAtlas; Q3ZCF0; -.
DR   PRIDE; Q3ZCF0; -.
DR   Ensembl; ENSBTAT00000014053; ENSBTAP00000014053; ENSBTAG00000010624.
DR   GeneID; 527201; -.
DR   KEGG; bta:527201; -.
DR   CTD; 10540; -.
DR   VEuPathDB; HostDB:ENSBTAG00000010624; -.
DR   VGNC; VGNC:27929; DCTN2.
DR   eggNOG; KOG3958; Eukaryota.
DR   GeneTree; ENSGT00390000003427; -.
DR   HOGENOM; CLU_049964_1_0_1; -.
DR   InParanoid; Q3ZCF0; -.
DR   OrthoDB; 951183at2759; -.
DR   TreeFam; TF105247; -.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000010624; Expressed in myometrium and 105 other tissues.
DR   ExpressionAtlas; Q3ZCF0; baseline.
DR   GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005869; C:dynactin complex; IBA:GO_Central.
DR   GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
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:0007017; P:microtubule-based process; IEA:InterPro.
DR   GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR   InterPro; IPR028133; Dynamitin.
DR   PANTHER; PTHR15346; PTHR15346; 1.
DR   Pfam; PF04912; Dynamitin; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Coiled coil; Cytoplasm; Cytoskeleton; Dynein; Membrane;
KW   Microtubule; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q13561"
FT   CHAIN           2..403
FT                   /note="Dynactin subunit 2"
FT                   /id="PRO_0000282604"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          184..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          100..130
FT                   /evidence="ECO:0000255"
FT   COILED          216..248
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         200
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13561"
FT   MOD_RES         322
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99KJ8"
SQ   SEQUENCE   403 AA;  44294 MW;  5F124BB01BB2CF47 CRC64;
     MADPKYADLP GIARNEPDVY ETSDLPEDDQ AEFDAEELTS TSVEHIIVNP NAAYDKFKDK
     RVGTKGLDFS DRIGKTKRTG YESGEYEMLG EGLGVKETPQ QKYQRLLHEV QELTTEVEKI
     KTTVKESATE EKLTPVVLAK QLAALKQQLV ASHLEKLLGP DAAINLTDPD GALAKRLLLQ
     LEATKNSKGT GSGGKTTSGT PPDSSLVTYE LHSRPEQDKF SQAAKVAELE KRLTELEATV
     RCDQDAQNPL SAGLQGACLM DTVELLQAKV GALDLAVLDQ VEARLQSVLG KVNEIAKHKA
     SVEDADTQSK VHQLYETIQR WSPIAASLPE LVQRLVTIKQ LHEQAMQFGQ LLTHLDTTQQ
     MIACSLKDNA TLLTQVQTTM CENLSTIEGN FANIDERMKK LGK