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Database: UniProt
Entry: A0A2I3G435_NOMLE
LinkDB: A0A2I3G435_NOMLE
Original site: A0A2I3G435_NOMLE 
ID   A0A2I3G435_NOMLE        Unreviewed;      1271 AA.
AC   A0A2I3G435;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Dynactin subunit 1 {ECO:0000256|ARBA:ARBA00016574};
GN   Name=DCTN1 {ECO:0000313|Ensembl:ENSNLEP00000026827.1};
OS   Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Nomascus.
OX   NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000026827.1, ECO:0000313|Proteomes:UP000001073};
RN   [1] {ECO:0000313|Ensembl:ENSNLEP00000026827.1, ECO:0000313|Proteomes:UP000001073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Gibbon Genome Sequencing Consortium;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNLEP00000026827.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC       {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the dynactin 150 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00011010}.
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DR   EMBL; ADFV01045809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01045810; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004090471.1; XM_004090423.2.
DR   AlphaFoldDB; A0A2I3G435; -.
DR   Ensembl; ENSNLET00000034685.1; ENSNLEP00000026827.1; ENSNLEG00000000385.3.
DR   GeneTree; ENSGT00940000155378; -.
DR   Proteomes; UP000001073; Chromosome 14.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR   InterPro; IPR036859; CAP-Gly_dom_sf.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   InterPro; IPR022157; Dynactin.
DR   PANTHER; PTHR18916; DYNACTIN 1-RELATED MICROTUBULE-BINDING; 1.
DR   PANTHER; PTHR18916:SF6; DYNACTIN SUBUNIT 1; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   Pfam; PF12455; Dynactin; 1.
DR   SMART; SM01052; CAP_GLY; 1.
DR   SUPFAM; SSF74924; Cap-Gly domain; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
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   Reference proteome {ECO:0000313|Proteomes:UP000001073}.
FT   DOMAIN          48..90
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          100..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          945..1036
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1271 AA;  140875 MW;  7327B17B44E78028 CRC64;
     MAQSKRHVYS RTPSGSRMSV EASARPLRVG SRVEVIGKGH RGTVAYVGAT LFATGKWVGV
     ILDEAKGKND GTVQGRKYFT CDEGHGIFVR QSQIQVFEDG ADTTSPETPD SSASKVLKRE
     GTDTTAKTSK LAPTARKTTA RRPKPTRPAS TGVAGASSSL GPSGSASAGE LSSSEPSTPA
     QTPLAAPIIP TPVLTSPGAV PPLPSPSKEE EGLRAQVRDL EEKLETLRLK RAEDKAKLKE
     LEKHKIQLEQ VQEWKSKMQE QQADLQRRLK EARKEAKEAL EAKERYMEEM ADTADAIEMA
     TLDKEMAEER AESLQQEVEA LKERVDELTT DLEILKAEIE EKGSDGAASS YQLKQLEEQN
     ARLKDALVRM RDLSSSEKQE HVKLQKLMEK KNQELEVVRQ QRERLQEELS QAESTIDELK
     EQVDAALGAE EMVEMLTDRN LNLEEKVREL RETVGDLEAM NEMNDELQEN ARETELELRE
     QLDMAGARVR EAQKRVEAAQ ETVADYQQTI KKYRQLTAHL QDVNRELTNQ QEASVERQQQ
     PPPETFDFKI KFAETKAHAK AIEMELRQME VAQANRHMSL LTAFMPDSFL RPGGDHDCVL
     VLLLMPRLIC KAELIRKQAQ EKFELSENCS ERPGLRGAAG EQLSFAAGLV YSLSLLQATL
     HRYEHALSQC SVDVYKKVGS LYPEMSAHER SLDFLIELLH KDQLDETVNV EPLTKAIKYY
     QHLYSIHLAE QPEDCTMQLA DHIKFTQSAL DCMSVEVGRL RAFLQGGQEA TDIALLLRDL
     ETSCSDIRQF CKKIRRRMPG TDAPGIPAAL AFGPQVSDTL LDCRKHLTWV VAVLQEVAAA
     AAQLIAPLAE NEGLPVAALE ELAFKASEQI YGIPSSSPYE CLRQSCNILI STMNKLATAM
     QEGEYDAERP PSKPPPVELR AAALRAEITD AEGLGLKLED RETVIKELKK SLKIKGEELS
     EANVRLSLLE KKLDSAAKDA DERIEKVQTR LEETQALLRK KEKEFEETMD ALQADIDQLE
     AEKAELKQRL NSQSKRTIEG LRGPPPSGIA TLVSGIAGEE QQRGAVPGQA PGSVPGPGLV
     KDSPLLLQQI SAMRLHISQL QHENSILKGA QMKASLASLP PLHVAKLSHE GPGSELPAGV
     LYRKTSQLLE TLNQLSTHTH VVDITRTSPA AKSPSAQLME QVAQLKSLSD TIEKLKDEVL
     KETVSQRPGA TVPTDFATFP SSAFLRAKEE QQDDTVYMGK VTFSCAAGLG QRHRLVLTQE
     QLHQLHSRLI S
//
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