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DRC1_BOVIN
ID   DRC1_BOVIN              Reviewed;         712 AA.
AC   Q32KY1; Q0V7L5;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Dynein regulatory complex protein 1;
DE   AltName: Full=Coiled-coil domain-containing protein 164;
GN   Name=DRC1; Synonyms=CCDC164;
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] (ISOFORM 2).
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC) a
CC       key regulator of ciliary/flagellar motility which maintains the
CC       alignment and integrity of the distal axoneme and regulates microtubule
CC       sliding in motile axonemes. Plays a critical role in the assembly of N-
CC       DRC and also stabilizes the assembly of multiple inner dynein arms and
CC       radial spokes. Coassembles with CCDC65/DRC2 to form a central scaffold
CC       needed for assembly of the N-DRC and its attachment to the outer
CC       doublet microtubules. {ECO:0000250|UniProtKB:P0DL09,
CC       ECO:0000250|UniProtKB:Q96MC2}.
CC   -!- SUBUNIT: Component of the nexin-dynein regulatory complex (N-DRC).
CC       {ECO:0000250|UniProtKB:P0DL09}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000250|UniProtKB:P0DL09}. Cytoplasm, cytoskeleton, flagellum
CC       axoneme {ECO:0000250|UniProtKB:P0DL09}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q32KY1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q32KY1-2; Sequence=VSP_023121;
CC   -!- SIMILARITY: Belongs to the DRC1 family. {ECO:0000305}.
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DR   EMBL; BT026555; ABH06342.1; -; mRNA.
DR   EMBL; BC109861; AAI09862.1; -; mRNA.
DR   RefSeq; NP_001032680.1; NM_001037591.1. [Q32KY1-1]
DR   AlphaFoldDB; Q32KY1; -.
DR   SMR; Q32KY1; -.
DR   STRING; 9913.ENSBTAP00000012714; -.
DR   PaxDb; Q32KY1; -.
DR   PRIDE; Q32KY1; -.
DR   Ensembl; ENSBTAT00000012714; ENSBTAP00000012714; ENSBTAG00000009649. [Q32KY1-1]
DR   Ensembl; ENSBTAT00000044033; ENSBTAP00000041552; ENSBTAG00000009649. [Q32KY1-2]
DR   GeneID; 509524; -.
DR   KEGG; bta:509524; -.
DR   CTD; 92749; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009649; -.
DR   eggNOG; ENOG502QQ2B; Eukaryota.
DR   GeneTree; ENSGT00940000153804; -.
DR   HOGENOM; CLU_012489_1_0_1; -.
DR   InParanoid; Q32KY1; -.
DR   OMA; LEKSECY; -.
DR   OrthoDB; 258073at2759; -.
DR   TreeFam; TF324985; -.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000009649; Expressed in oviduct epithelium and 74 other tissues.
DR   ExpressionAtlas; Q32KY1; baseline.
DR   GO; GO:0005858; C:axonemal dynein complex; IEA:InterPro.
DR   GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR   GO; GO:0070286; P:axonemal dynein complex assembly; IMP:UniProtKB.
DR   GO; GO:0060285; P:cilium-dependent cell motility; IMP:UniProtKB.
DR   GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0003352; P:regulation of cilium movement; IBA:GO_Central.
DR   InterPro; IPR039505; DRC1/2_N.
DR   InterPro; IPR039750; DRC1/DRC2.
DR   InterPro; IPR029440; DRC1_C.
DR   PANTHER; PTHR21625; PTHR21625; 1.
DR   Pfam; PF14772; NYD-SP28; 1.
DR   Pfam; PF14775; NYD-SP28_assoc; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell projection; Cilium; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Flagellum; Reference proteome.
FT   CHAIN           1..712
FT                   /note="Dynein regulatory complex protein 1"
FT                   /id="PRO_0000277880"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          100..388
FT                   /evidence="ECO:0000255"
FT   COILED          663..698
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        563..586
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         227..296
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16305752"
FT                   /id="VSP_023121"
FT   CONFLICT        344
FT                   /note="L -> P (in Ref. 1; ABH06342)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   712 AA;  84070 MW;  B508E33F1CD311E3 CRC64;
     MNPPGSLGVL EEKEEEHLAP PILGPSIHSD NPQERIQARR LRIAARLEAR RREALGEYLD
     GKKESEEDQS KSYKQKEESR LKLAKLLLCG TELVTNIQVA ADIREIHRRV EEEEIKRQRL
     EKLENEVKTS QDKFDEITVK WEEGKQRRIP QELWEMLNAQ QVHCAGLIED KNKLISELQQ
     ELKMKDDQYV KDLKKQSDDI CLLLERMEEQ VKNVMKTFRQ ELQNIEKAFE VERQELLTSN
     KKKWERALQA HNAKELEYLM NRIKKVEDYE KQLNKQRIWD CEEYNTIKIK LEQDVQILEQ
     QLQQMKATYQ LNQEKLEYNF QVLKKRDEES TVIKSQQKRK INRLHDVLNN LRSKYNKQVK
     QFQEENQSLT SDYKRLVLQF KELQKAMRHF ALIDDKRFRE IWLMNEEEAK DLINRAFDVD
     RIISTHHLGL PWMAPDFWFL KNVGPISQQQ QKSATQILEE VLMEAEKEGA DEDSSESETY
     LDLPKQVSAR TTRKILMLLC DESGFLIESK LLSLLLPLEK NECYLLRLDA VFSALGIENE
     DDLYKLVNFF LKYQTHHSPS SQEPLDLRAE KERSLVDGKS QEKEPPPSPK LIHPNDVLKI
     LEAFVMSLRK PRDFWVPVKL LKAVRDDSKD SEYWEALTTV IPATTLNLWD ALYTALEKYH
     LVLTQRAELL IENSSLERQN TELQQLLQQY LDTKINSELQ VPPTQVFRVP TK
 
 
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