DYH12_BOVIN
ID DYH12_BOVIN Reviewed; 356 AA.
AC Q58CT0; A6QNK5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Dynein axonemal heavy chain 12;
DE AltName: Full=Ankyrin repeat and SOCS box protein 14;
DE Short=ASB-14;
DE AltName: Full=Axonemal beta dynein heavy chain 12;
DE AltName: Full=Ciliary dynein heavy chain 12;
GN Name=DNAH12; Synonyms=ASB14;
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].
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].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Force generating protein of respiratory cilia. Produces force
CC towards the minus ends of microtubules. Dynein has ATPase activity; the
CC force-producing power stroke is thought to occur on release of ADP.
CC Involved in sperm motility; implicated in sperm flagellar assembly (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: May be a substrate-recognition component of a SCF-like ECS
CC (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex
CC which mediates the ubiquitination and subsequent proteasomal
CC degradation of target proteins. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC intermediate and light chains.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced.;
CC Name=1;
CC IsoId=Q58CT0-1; Sequence=Displayed;
CC -!- DOMAIN: Dynein heavy chains probably consist of an N-terminal stem
CC (which binds cargo and interacts with other dynein components), and the
CC head or motor domain. The motor contains six tandemly-linked AAA
CC domains in the head, which form a ring. A stalk-like structure (formed
CC by two of the coiled coil domains) protrudes between AAA 4 and AAA 5
CC and terminates in a microtubule-binding site. A seventh domain may also
CC contribute to this ring; it is not clear whether the N-terminus or the
CC C-terminus forms this extra domain. There are four well-conserved and
CC two non-conserved ATPase sites, one per AAA domain. Probably only one
CC of these (within AAA 1) actually hydrolyzes ATP, the others may serve a
CC regulatory function (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The SOCS box domain mediates the interaction with the Elongin
CC BC complex, an adapter module in different E3 ubiquitin-protein ligase
CC complexes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
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DR EMBL; BT021867; AAX46714.1; -; mRNA.
DR EMBL; BC148874; AAI48875.1; -; mRNA.
DR RefSeq; NP_001030242.2; NM_001035070.2.
DR AlphaFoldDB; Q58CT0; -.
DR SMR; Q58CT0; -.
DR STRING; 9913.ENSBTAP00000021315; -.
DR PaxDb; Q58CT0; -.
DR GeneID; 509431; -.
DR KEGG; bta:509431; -.
DR CTD; 142686; -.
DR eggNOG; KOG0504; Eukaryota.
DR HOGENOM; CLU_023739_1_0_1; -.
DR InParanoid; Q58CT0; -.
DR OrthoDB; 311534at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF07525; SOCS_box; 1.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00253; SOCS; 1.
DR SMART; SM00969; SOCS_box; 1.
DR SUPFAM; SSF158235; SSF158235; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50225; SOCS; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ANK repeat; ATP-binding; Cell projection; Cilium;
KW Coiled coil; Cytoplasm; Cytoskeleton; Dynein; Microtubule; Motor protein;
KW Nucleotide-binding; Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..356
FT /note="Dynein axonemal heavy chain 12"
FT /id="PRO_0000285853"
FT REPEAT 17..46
FT /note="ANK 1"
FT REPEAT 50..81
FT /note="ANK 2"
FT REPEAT 82..111
FT /note="ANK 3"
FT REPEAT 124..153
FT /note="ANK 4"
FT REPEAT 154..183
FT /note="ANK 5"
FT REPEAT 185..218
FT /note="ANK 6"
FT DOMAIN 290..345
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
SQ SEQUENCE 356 AA; 39862 MW; EE57F83D569FE5DB CRC64;
MELLLQKGAN ALGQASDSSS ILLEAASGGN PDSVTLLLEY GADANVPKNS GHLPIHVAAD
RGHLLALKTL VPVTDFAAIK RSGISPIHCA AAGAHPKCLE LLIQAGFDVN FMLDQRIRKH
YDDHRKSALY FAVSNGDLSS VKLLLSAGAM PNQDPVNCLQ IALRMGNYEL VSLLLRHGAN
VNYFCRVNPL HFPSALQYTL KDEVMLRMLL NYGYDTELCF DCPHGDKVHR FSASEGWTST
VIKDTMFCEV ITLSWLQHLS GKVVRVMLDY VDQVRICSKL KAVLQKQGLW SEIHFILTNP
RSLKHLCRLK IRKCMGRLRL RCPVFMSFLP LPSRLKAYVL YKEYDLYEQG IFTGTW
