CNBD2_MOUSE
ID CNBD2_MOUSE Reviewed; 673 AA.
AC Q9D5U8; A2ATV2; Q8R083;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Cyclic nucleotide-binding domain-containing protein 2;
DE AltName: Full=Cyclic nucleotide receptor involved in sperm function {ECO:0000303|PubMed:24339785};
GN Name=Cnbd2; Synonyms=Cris {ECO:0000303|PubMed:24339785};
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 MRNA] OF 35-673 (ISOFORM 2).
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24339785; DOI=10.1371/journal.pgen.1003960;
RA Kraehling A.M., Alvarez L., Debowski K., Van Q., Gunkel M., Irsen S.,
RA Al-Amoudi A., Struenker T., Kremmer E., Krause E., Voigt I., Woertge S.,
RA Waisman A., Weyand I., Seifert R., Kaupp U.B., Wachten D.;
RT "CRIS-a novel cAMP-binding protein controlling spermiogenesis and the
RT development of flagellar bending.";
RL PLoS Genet. 9:E1003960-E1003960(2013).
CC -!- FUNCTION: Essential for male fertility. Plays an important role in
CC spermatogenesis and regulates sperm motility by controlling the
CC development of the flagellar bending of sperm (PubMed:24339785).
CC {ECO:0000269|PubMed:24339785}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24339785}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D5U8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D5U8-2; Sequence=VSP_003825;
CC -!- TISSUE SPECIFICITY: Testis-specific. Exclusively expressed in
CC testicular germ cells while it is not present in mature sperm (at
CC protein level). {ECO:0000269|PubMed:24339785}.
CC -!- DISRUPTION PHENOTYPE: Males are either infertile due to a lack of sperm
CC resulting from spermatogenic arrest, or subfertile due to impaired
CC sperm motility. The motility defect is caused by altered Ca(2+)
CC regulation of the flagellar beat of sperm.
CC {ECO:0000269|PubMed:24339785}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27204.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK014912; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL928935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027204; AAH27204.1; ALT_INIT; mRNA.
DR CCDS; CCDS50778.1; -. [Q9D5U8-1]
DR RefSeq; NP_081861.2; NM_027585.2. [Q9D5U8-1]
DR AlphaFoldDB; Q9D5U8; -.
DR SMR; Q9D5U8; -.
DR STRING; 10090.ENSMUSP00000041268; -.
DR iPTMnet; Q9D5U8; -.
DR PhosphoSitePlus; Q9D5U8; -.
DR MaxQB; Q9D5U8; -.
DR PaxDb; Q9D5U8; -.
DR PRIDE; Q9D5U8; -.
DR ProteomicsDB; 283448; -. [Q9D5U8-1]
DR ProteomicsDB; 283449; -. [Q9D5U8-2]
DR Antibodypedia; 51163; 52 antibodies from 14 providers.
DR Ensembl; ENSMUST00000037096; ENSMUSP00000041268; ENSMUSG00000038085. [Q9D5U8-1]
DR GeneID; 70873; -.
DR KEGG; mmu:70873; -.
DR UCSC; uc008nnd.2; mouse. [Q9D5U8-1]
DR UCSC; uc008nne.2; mouse. [Q9D5U8-2]
DR CTD; 140894; -.
DR MGI; MGI:1918123; Cnbd2.
DR VEuPathDB; HostDB:ENSMUSG00000038085; -.
DR eggNOG; KOG1113; Eukaryota.
DR GeneTree; ENSGT00390000003964; -.
DR InParanoid; Q9D5U8; -.
DR OMA; IMMIRVC; -.
DR OrthoDB; 1253607at2759; -.
DR PhylomeDB; Q9D5U8; -.
DR TreeFam; TF326269; -.
DR BioGRID-ORCS; 70873; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Cnbd2; mouse.
DR PRO; PR:Q9D5U8; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9D5U8; protein.
DR Bgee; ENSMUSG00000038085; Expressed in spermatid and 87 other tissues.
DR ExpressionAtlas; Q9D5U8; baseline and differential.
DR Genevisible; Q9D5U8; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0030552; F:cAMP binding; IDA:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR043533; CNBD1/2.
DR InterPro; IPR038897; CNBD2.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR23011; PTHR23011; 1.
DR PANTHER; PTHR23011:SF35; PTHR23011:SF35; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; SSF51206; 2.
DR PROSITE; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; cAMP; cAMP-binding; Cytoplasm; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..673
FT /note="Cyclic nucleotide-binding domain-containing protein
FT 2"
FT /id="PRO_0000079473"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 206..329
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT VAR_SEQ 172..183
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_003825"
FT CONFLICT 476
FT /note="F -> Y (in Ref. 3; AAH27204)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="L -> P (in Ref. 3; AAH27204)"
FT /evidence="ECO:0000305"
FT CONFLICT 591
FT /note="R -> Q (in Ref. 3; AAH27204)"
FT /evidence="ECO:0000305"
FT CONFLICT 657
FT /note="H -> Q (in Ref. 1; AK014912)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 673 AA; 77892 MW; B316EA21E109FE17 CRC64;
MNRSANPEAA SSTSHVKFDL GKSVDISSTD TKDGGTARSP LEPADKSDTT ESKSESGSDS
RSEEDKESPA SIKEIKAETP QPKDRPGVQI KLSWSQKIKS WTAKKKRKLY QLVIDIIMMN
RVCKMFRQGL RGFREYQIIE PVHKKHPDFS FWDKKKQGRI SFVTEDFAAQ EGHFPPRAIS
ITQKKPSWRT HQEIQDLCNI LQALDCYRSY TESLQLLLAK VIRFERFGRR RVIVKKGQMG
NSFYFIYLGT VAITEDEDGS SAFLDPHPTL LHRGGSFGEM GLLSTTVRSA TVVCMEETEF
LVVDREDFVA NKLGDEVQKE TQYRYNFFRN LDIFQSWSEE KLWKLVALGR IERFSYGQMV
SKDFMNSAFI TFICQGNCEI LRLVALGDCS AYYKWVWQQL ELLDHKPLRI HDNEISPKER
FKELQIKSYP LQDFTYLKLL RLQKAREQQG IDFHGKINKV ENTLPKLLGP KIKSRFGHLV
KCSMVNTKFG ELPKEAIVGV YMKIHKTEEG EIVGLHQAFV PEIQRDCRPF ILLSLGSELI
QVRKEKFYDM VDEETRAKII KMDVDYPSDE DLCQSFLKEN DYIVFRKDLL RLLVEPLNKS
PFIPVQTKKK EIYNHKSLFL DLCSLEKKVK QHYPIFLAPQ KYLPPLRVVQ AISAPRHKIQ
ELLPQYKNAG VLI
