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Database: UniProt
Entry: A0A1S3N8U5_SALSA
LinkDB: A0A1S3N8U5_SALSA
Original site: A0A1S3N8U5_SALSA 
ID   A0A1S3N8U5_SALSA        Unreviewed;      1245 AA.
AC   A0A1S3N8U5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Dynactin subunit 1 {ECO:0000256|ARBA:ARBA00016574};
GN   Name=LOC106577911 {ECO:0000313|RefSeq:XP_014011832.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014011832.1};
RN   [1] {ECO:0000313|RefSeq:XP_014011832.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014011832.1};
RG   RefSeq;
RL   Submitted (SEP-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   RefSeq; XP_014011832.1; XM_014156357.1.
DR   AlphaFoldDB; A0A1S3N8U5; -.
DR   OrthoDB; 9423at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa18.
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:UP000087266}.
FT   DOMAIN          31..73
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   REGION          84..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          959..1011
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1059..1086
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        84..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..137
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..174
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1245 AA;  137434 MW;  965966689F391CD8 CRC64;
     MSADGGGKPA KVGSVVEVIG KGQRGTVAYV GATLFATGKW VGVILDEPKG KNDGTVQGKR
     YFQCDENCGI FVRQSQIQLV EDGVTSPDIP ESSTAKFLSK QKDMPEIPKS VKQSVTRRST
     KAPRAIGLSS SRSREDVSEG SLSSKGALGA PVVPLPSGAP ATSGAPPPAT PSKAEPPASK
     QEEESLRGQV KDLEEKLETL KMKRAEDKVK LKELEKHKIQ LEQLQEWKTK MQEQQTDLQK
     QLKEAKKDAR EALEAKDRYM EEMSDTADAI EMATLDKEMA EERSESLQVE VESLKEKVEE
     LTMDLEIIKH EVEEKGSDGA ASSYHVKQLE EQNSRLKDAL VRMRDLSSSE KQEHVKLQKQ
     MEKKNGELET LRTQKEKLQE EMKQAEATID ELKEQVDAAL GAEEMVETLT ERNLDLEEKV
     RELRETVTDL EAINEMNDEL QENSRETEME LREQLDLNGA RVREAQKRVE AAQETVADYQ
     QTINKYRQLT ASLQDANKEL TSAQNANAEQ VQQPPAELFD FKIKFAETKA YAKAIEMELR
     KMEVGQANRQ VSLLTSFMPD SFLRHGGDHD CILVLLLIPR LICKAELISK QAQEKFDLNG
     NPVERTGVKM RGPPGEQLSF ASGLVYSLTL LQATLHKYQQ ALNCCSVQVY MQMGTLYSEM
     SVHERSLDFF IDLLHKDQLD ETVHVEPLTK AIKYYQQLYS IHLAEQTEDC TVQLADHIKF
     IQSALDCIGA EVVRLRAFLQ PGQEGLALNI LLKDLDTTCS DIKQFCKKIR RRMPGTDVPG
     VPAALSFGAP VSETLTDCRR QLTRVVAVLQ EVAAAGAQMV APLGEQEGLN ALKLDDVAFK
     AVEQVYGSQG LNPHECLRQS CSAVISTMNK MATAMQEGEY DAERPQGKAP PVEARAAALR
     AEITDAEGLG VKLEDRDTVI KELKKSLKIK GEELSEAHVR LSLLEKKLDT STKDADERVE
     KIQTKLDETL ALLKKKEKEF EETMDALQAD IDQLEAEKAE LKQRLSSQSK STIEGLRAPP
     ASGIASIVTG SAGAALAPGA GGLSGPMQVV DSPLLRQQVE AQRLGIKHLK NENNRLKAEK
     MRAQLASLPP LHVPKLHLRE ATSSSSPPAE GPLQGALYRK TEQLLGTLLK MTATVKVVDI
     TGKTPVSASA QLLDQTARLQ SLSDALDKLK GEVAEHVVSQ QPGAKVSSDF ATFPISSFVK
     AKEEKQGGTV FVGRVAIPCA KGQEQVHRLV LSQQHLQQVH RLLIA
//
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