DCTN1_XENLA
ID DCTN1_XENLA Reviewed; 1232 AA.
AC Q6PCJ1;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Dynactin subunit 1;
GN Name=dctn1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a key role in dynein-mediated retrograde transport of
CC vesicles and organelles along microtubules by recruiting and tethering
CC dynein to microtubules. Binds to both dynein and microtubules providing
CC a link between specific cargos, microtubules and dynein. Plays a role
CC in metaphase spindle orientation. {ECO:0000250|UniProtKB:Q14203}.
CC -!- SUBUNIT: Binds to microtubules and to cytoplasmic dynein. Binds
CC preferentially to tyrosinated microtubules than to detyrosinated
CC microtubules. {ECO:0000250|UniProtKB:Q14203}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14203}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q14203}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q14203}. Note=Localizes to microtubule plus
CC ends. Localizes preferentially to tyrosinated microtubules than to
CC detyrosinated microtubules. {ECO:0000250|UniProtKB:Q14203}.
CC -!- SIMILARITY: Belongs to the dynactin 150 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; BC059305; AAH59305.1; -; mRNA.
DR RefSeq; NP_001080006.1; NM_001086537.1.
DR AlphaFoldDB; Q6PCJ1; -.
DR SMR; Q6PCJ1; -.
DR IntAct; Q6PCJ1; 3.
DR PRIDE; Q6PCJ1; -.
DR GeneID; 379696; -.
DR KEGG; xla:379696; -.
DR CTD; 379696; -.
DR Xenbase; XB-GENE-5933563; dctn1.L.
DR OMA; ADKNMRY; -.
DR OrthoDB; 1550378at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 379696; Expressed in brain and 19 other tissues.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0099738; C:cell cortex region; ISS:UniProtKB.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISS:UniProtKB.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISS:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; ISS:UniProtKB.
DR Gene3D; 2.30.30.190; -; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR022157; Dynactin.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF12455; Dynactin; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; SSF74924; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton; Dynein;
KW Microtubule; Mitosis; Reference proteome.
FT CHAIN 1..1232
FT /note="Dynactin subunit 1"
FT /id="PRO_0000083522"
FT DOMAIN 31..73
FT /note="CAP-Gly"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT REGION 82..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..505
FT /evidence="ECO:0000255"
FT COILED 908..1005
FT /evidence="ECO:0000255"
FT COILED 1046..1071
FT /evidence="ECO:0000255"
FT COILED 1136..1166
FT /evidence="ECO:0000255"
FT COMPBIAS 111..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1232 AA; 137285 MW; ED5FC8DA07C93018 CRC64;
MSVEATGKPL KVGSRVEVIG KGYRGTVAYV GATLFATGKW VGVILDDSKG KNDGTVQGRR
YFTCEENHGI FVRQSQIQVI EDGADTTSPE TPEPTASKGL KKDVMETPKS SKLPTRPSSS
AASSGTASAS CGEISSSEPS TPAQTPLAAP IIPSPSSAIT SPVAPLPGPG PSKEEENLRA
QVKDLEEKLE TLKMKRAEDK AKLKEMEKSK LQLEQVQEWK SKMQEQQADI QRQLKEAKKE
AKEALEAKER YMEEMADTAD AIEMATLDKE MAEERAESLQ QEVDTLKDKV EEHKIDLEIL
KHEIEEKGSD GAASSYQVKQ LEEQNARLKE ALVRMRDLSA SEKQEHIKVQ KQMEKKNTEL
DTLRQQKEKL QEEASHMEKT IDELKEQVDA ALGAEEMVET LAERNLDLEE KVRELRETVS
DLEAINEMND ELQENARETE LELREQLDMA GARVREAEKR VEAAQETVAD YQQTIKKYRD
LTAHLQEVNS ELRNQQEASV EKEQQPSPEM FDFKIKFAET KAHAKAIEME LRKMEVTQAN
RHVSLLTSFM PDSFLRHGGD HDCILVLLLI PRLICKAELI SKQAQEKFEL SEVGEQKSGM
RGAVGEQMSF AAGLVYSLTL LQATLHKYEQ ALDKCSVEVY KKVGMLYPEM SVHERSLDFL
IELLHKDQLD ETVNVEPLTK AIKYYQHLYS IHLADQAEEC TMQLSDHIKF TQSALDCMGV
EVSRLRAFLH AGQESSDFAI LLKDLETSCS DIRQFCKKIR RRMPGTEAAG IPAALGFGQQ
VCETLLDCRK YLKCVVAVFQ EVAAAGAQMI APMGENEGLQ ALKLEDVAFK ATEQIYGTKG
SNPYECLRQS CSVVIATMNK MATAMQEGEY DAEKPQSKSP PPVEQRAAAL RAEITDAEGL
GLKLEDRETV IKELKKSLKI KGEELSEANV RLSLLEKKLD SASKEADDRV EKIQTKLEET
QTVLKKKEKE FEETMDALQA DIDQLESEKA ELRQRLNNQS KRTIEGLRGV PASGVASIVS
GLAGGVSSGQ SLINGSGPVQ VKDSPLLLQQ IDALRLSMKH LKHENNKLKA HQIKTDLSSL
PALHVPKLTL PKDRQKEEAM SGTLYRKTSQ LLDALQQMSA NAKVVDITHK KAGNPAAQLL
EQTARLKSLS DTIDKLKNEV MKETVSQCPG ANVPTDFATF PSTDFIKAKE EKKEDTVYIG
KVTLSCQPGQ GQIHKLVLTP EQLHELHERL IC
