ID   DYDC1_MOUSE             Reviewed;         175 AA.
AC   Q9D9T0; G3X8U6; Q810Q6;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   29-MAY-2024, entry version 115.
DE   RecName: Full=DPY30 domain-containing protein 1;
GN   Name=Dydc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION.
RX   PubMed=19545932; DOI=10.1016/j.ejcb.2009.05.001;
RA   Li S., Qiao Y., Di Q., Le X., Zhang L., Zhang X., Zhang C., Cheng J.,
RA   Zong S., Koide S.S., Miao S., Wang L.;
RT   "Interaction of SH3P13 and DYDC1 protein: a germ cell component that
RT   regulates acrosome biogenesis during spermiogenesis.";
RL   Eur. J. Cell Biol. 88:509-520(2009).
RN   [6]
RP   FUNCTION, IDENTIFICATION IN RADIAL SPOKE COMPLEX 1, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=36417862; DOI=10.1016/j.celrep.2022.111683;
RA   Zhang X., Xiao Z., Zhang J., Xu C., Liu S., Cheng L., Zhou S., Zhao S.,
RA   Zhang Y., Wu J., Wang Y., Liu M.;
RT   "Differential requirements of IQUB for the assembly of radial spoke 1 and
RT   the motility of mouse cilia and flagella.";
RL   Cell Rep. 41:111683-111683(2022).
CC   -!- FUNCTION: Functions as part of axonemal radial spoke complexes that
CC       play an important part in the motility of sperm and cilia
CC       (PubMed:36417862). Plays a crucial role during acrosome biogenesis
CC       (PubMed:19545932). {ECO:0000269|PubMed:19545932,
CC       ECO:0000269|PubMed:36417862}.
CC   -!- SUBUNIT: Component of the axonemal radial spoke complex 1 (RS1), at
CC       least composed of spoke head proteins RSPH1, RSPH3, RSPH9 and the
CC       cilia-specific component RSPH4A or sperm-specific component RSPH6A,
CC       spoke stalk proteins RSPH14, DNAJB13, DYDC1, ROPN1L and NME5, and the
CC       anchor protein IQUB (PubMed:36417862). Interacts with SH3GL3 (By
CC       similarity). {ECO:0000250|UniProtKB:Q8WWB3,
CC       ECO:0000269|PubMed:36417862}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme
CC       {ECO:0000305|PubMed:36417862}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9D9T0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D9T0-2; Sequence=VSP_020012;
CC   -!- SIMILARITY: Belongs to the dpy-30 family. {ECO:0000305}.
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DR   EMBL; AK006511; BAB24626.1; -; mRNA.
DR   EMBL; AC154597; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466573; EDL24916.1; -; Genomic_DNA.
DR   EMBL; BC049632; AAH49632.1; -; mRNA.
DR   CCDS; CCDS49451.1; -. [Q9D9T0-1]
DR   RefSeq; NP_081370.1; NM_027094.1. [Q9D9T0-1]
DR   AlphaFoldDB; Q9D9T0; -.
DR   SMR; Q9D9T0; -.
DR   BioGRID; 213484; 2.
DR   ComplexPortal; CPX-8161; Radial spoke complex, ciliiar variant.
DR   ComplexPortal; CPX-8162; Radial spoke complex, flagellar variant.
DR   STRING; 10090.ENSMUSP00000139412; -.
DR   iPTMnet; Q9D9T0; -.
DR   PhosphoSitePlus; Q9D9T0; -.
DR   PaxDb; 10090-ENSMUSP00000124785; -.
DR   ProteomicsDB; 279586; -. [Q9D9T0-1]
DR   ProteomicsDB; 279587; -. [Q9D9T0-2]
DR   Antibodypedia; 29980; 188 antibodies from 29 providers.
DR   Ensembl; ENSMUST00000022315.12; ENSMUSP00000022315.6; ENSMUSG00000021790.13. [Q9D9T0-1]
DR   Ensembl; ENSMUST00000189865.7; ENSMUSP00000139412.2; ENSMUSG00000021790.13. [Q9D9T0-1]
DR   GeneID; 69496; -.
DR   KEGG; mmu:69496; -.
DR   UCSC; uc007tcl.2; mouse. [Q9D9T0-1]
DR   AGR; MGI:1916746; -.
DR   CTD; 143241; -.
DR   MGI; MGI:1916746; Dydc1.
DR   VEuPathDB; HostDB:ENSMUSG00000021790; -.
DR   eggNOG; ENOG502S3U3; Eukaryota.
DR   GeneTree; ENSGT00940000161631; -.
DR   InParanoid; Q9D9T0; -.
DR   OrthoDB; 5491730at2759; -.
DR   BioGRID-ORCS; 69496; 3 hits in 76 CRISPR screens.
DR   PRO; PR:Q9D9T0; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q9D9T0; Protein.
DR   Bgee; ENSMUSG00000021790; Expressed in spermatid and 18 other cell types or tissues.
DR   ExpressionAtlas; Q9D9T0; baseline and differential.
DR   GO; GO:0097729; C:9+2 motile cilium; IC:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:GOC.
DR   GO; GO:0001534; C:radial spoke; IDA:UniProtKB.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IBA:GO_Central.
DR   GO; GO:0036126; C:sperm flagellum; IC:UniProtKB.
DR   GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; IC:UniProtKB.
DR   GO; GO:0030317; P:flagellated sperm motility; IC:UniProtKB.
DR   GO; GO:0007618; P:mating; IC:UniProtKB.
DR   CDD; cd22966; DD_DYDC-like; 1.
DR   Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR   InterPro; IPR007858; Dpy-30_motif.
DR   InterPro; IPR049630; DYDC-like_DD.
DR   InterPro; IPR037856; Sdc1/DPY30.
DR   PANTHER; PTHR23356:SF4; DPY30 DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR23356; DPY30-RELATED; 1.
DR   Pfam; PF05186; Dpy-30; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; Cilium; Cytoplasm; Cytoskeleton;
KW   Flagellum; Reference proteome.
FT   CHAIN           1..175
FT                   /note="DPY30 domain-containing protein 1"
FT                   /id="PRO_0000247557"
FT   REGION          94..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          152..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         69..84
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_020012"
FT   CONFLICT        152
FT                   /note="A -> E (in Ref. 1; BAB24626)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   175 AA;  20494 MW;  45EAB6A38F877069 CRC64;
     MESRYLQKCL GTCLTQGLTE VARVRPLDPI EYLAFWLYKH KENMNMEQMR QREMITLEHE
     RELAMMEQEM LERLKAEELL FQQQLAFQLE LEMQQKEKQK SEDFETGQEK SFKSMMSMES
     TARGEEQEPM QAEELVMDSG KTLAEISDRY GAPNLSRVEE LDEPMLSDNG VSAPP
//