CBY2_MOUSE
ID CBY2_MOUSE Reviewed; 446 AA.
AC Q32MG2; Q8CIV5; Q9D9E6; Q9D9Z0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Protein chibby homolog 2 {ECO:0000305};
DE AltName: Full=Protein nurit;
DE AltName: Full=Spermatid-associated protein;
GN Name=Cby2; Synonyms=Nurit, Spert;
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 [MRNA] (ISOFORM 3), INTERACTION WITH NEK1,
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=CD-1;
RX PubMed=12204287; DOI=10.1016/s0925-4773(02)00217-4;
RA Feige E., Chen A., Motro B.;
RT "Nurit, a novel leucine-zipper protein, expressed uniquely in the spermatid
RT flower-like structure.";
RL Mech. Dev. 117:369-377(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=33536340; DOI=10.1073/pnas.2018355118;
RA Shimada K., Park S., Miyata H., Yu Z., Morohoshi A., Oura S., Matzuk M.M.,
RA Ikawa M.;
RT "ARMC12 regulates spatiotemporal mitochondrial dynamics during
RT spermiogenesis and is required for male fertility.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC -!- SUBUNIT: Homodimer. Binds to NEK1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q32MG2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q32MG2-2; Sequence=VSP_028676, VSP_028677;
CC Name=3;
CC IsoId=Q32MG2-3; Sequence=VSP_028675;
CC -!- TISSUE SPECIFICITY: Testis-specific (PubMed:33536340). Expression is
CC restricted to the flower-like structure in spermatids.
CC {ECO:0000269|PubMed:12204287, ECO:0000269|PubMed:33536340}.
CC -!- DEVELOPMENTAL STAGE: Expressed through the elongation stage of the
CC spermatids but absent from mature spermatozoa.
CC {ECO:0000269|PubMed:12204287}.
CC -!- SIMILARITY: Belongs to the chibby family. SPERT subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB24530.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY092416; AAM18190.1; -; mRNA.
DR EMBL; AK006329; BAB24530.1; ALT_INIT; mRNA.
DR EMBL; AK007022; BAB24833.1; -; mRNA.
DR EMBL; AC125205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC109147; AAI09148.1; -; mRNA.
DR CCDS; CCDS27279.1; -. [Q32MG2-2]
DR CCDS; CCDS49541.1; -. [Q32MG2-3]
DR CCDS; CCDS49543.1; -. [Q32MG2-1]
DR RefSeq; NP_001157611.1; NM_001164139.1. [Q32MG2-1]
DR RefSeq; NP_001157613.1; NM_001164141.1. [Q32MG2-3]
DR RefSeq; NP_080733.2; NM_026457.2. [Q32MG2-2]
DR RefSeq; XP_006519543.1; XM_006519480.1.
DR RefSeq; XP_011243469.1; XM_011245167.1. [Q32MG2-3]
DR RefSeq; XP_011243470.1; XM_011245168.1. [Q32MG2-3]
DR AlphaFoldDB; Q32MG2; -.
DR SMR; Q32MG2; -.
DR STRING; 10090.ENSMUSP00000127439; -.
DR iPTMnet; Q32MG2; -.
DR PhosphoSitePlus; Q32MG2; -.
DR PaxDb; Q32MG2; -.
DR PRIDE; Q32MG2; -.
DR ProteomicsDB; 258716; -. [Q32MG2-1]
DR ProteomicsDB; 258717; -. [Q32MG2-2]
DR ProteomicsDB; 258718; -. [Q32MG2-3]
DR Antibodypedia; 42238; 67 antibodies from 15 providers.
DR DNASU; 67926; -.
DR Ensembl; ENSMUST00000035243; ENSMUSP00000046259; ENSMUSG00000034913. [Q32MG2-2]
DR Ensembl; ENSMUST00000164082; ENSMUSP00000127439; ENSMUSG00000034913. [Q32MG2-1]
DR Ensembl; ENSMUST00000165569; ENSMUSP00000131347; ENSMUSG00000034913. [Q32MG2-3]
DR GeneID; 67926; -.
DR KEGG; mmu:67926; -.
DR UCSC; uc007uqu.2; mouse. [Q32MG2-2]
DR UCSC; uc011zon.1; mouse. [Q32MG2-1]
DR CTD; 220082; -.
DR MGI; MGI:1915176; Cby2.
DR VEuPathDB; HostDB:ENSMUSG00000034913; -.
DR eggNOG; ENOG502S6IZ; Eukaryota.
DR GeneTree; ENSGT00940000153137; -.
DR HOGENOM; CLU_041289_0_0_1; -.
DR InParanoid; Q32MG2; -.
DR OMA; WSIWEEN; -.
DR OrthoDB; 1015941at2759; -.
DR PhylomeDB; Q32MG2; -.
DR TreeFam; TF324419; -.
DR BioGRID-ORCS; 67926; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q32MG2; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q32MG2; protein.
DR Bgee; ENSMUSG00000034913; Expressed in seminiferous tubule of testis and 13 other tissues.
DR ExpressionAtlas; Q32MG2; baseline and differential.
DR Genevisible; Q32MG2; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR CDD; cd07429; Cby_like; 1.
DR InterPro; IPR028118; Chibby_fam.
DR InterPro; IPR026655; SPERT.
DR PANTHER; PTHR21533:SF13; PTHR21533:SF13; 1.
DR Pfam; PF14645; Chibby; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Phosphoprotein; Reference proteome.
FT CHAIN 1..446
FT /note="Protein chibby homolog 2"
FT /id="PRO_0000307293"
FT REGION 208..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 161..197
FT /evidence="ECO:0000255"
FT COILED 236..264
FT /evidence="ECO:0000255"
FT COILED 353..411
FT /evidence="ECO:0000255"
FT COMPBIAS 209..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AXV6"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AXV6"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AXV6"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AXV6"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AXV6"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AXV6"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AXV6"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AXV6"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AXV6"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AXV6"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AXV6"
FT VAR_SEQ 1..78
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12204287"
FT /id="VSP_028675"
FT VAR_SEQ 1..36
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_028676"
FT VAR_SEQ 37..51
FT /note="TRSESLEIPVNVILP -> MQPEGVKCRMEGPKA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_028677"
FT CONFLICT 82
FT /note="R -> T (in Ref. 2; BAB24833)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="D -> E (in Ref. 2; BAB24530)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 446 AA; 51865 MW; 25E4203B9B7CEA42 CRC64;
MSPLECSECF GDQLLHKTYT WHLTLHSRPN FTRKRDTRSE SLEIPVNVIL PQRGTEPFLR
LHNLYSTPRC SRQAALPRMS RRVASQHSYP LNRFSSMPFD PMERPTSQAD LELDYNPPRV
QLSDEMFVFQ DGRWVNESCR LQPPYFSPPS SFHHKLHHRR LAKEYQLQEE NKSLRDENRA
LRDENKALRK ENKILQVFWE EHKVTLGHEE SQTSSLLHKD TTSQEVVKRD NTTLPAQRSK
ESTLQLIREE NRALQQLLEQ RQAYWAQAEE NAASTEEGKS TSSPKEESHN SGLLPDQSTN
HSSPFEDPKV PPTTQEDSKT LRALREMVNN LSGASGEEDG KVGPNLPDSA QPLQLLREMN
QALQALQEEN RLLQEENRAL HILREEHRVF QEENKALWEN NKLKLQQRLV IDTVTEVTAR
MEMLIEELYA FMPAKNNKDP KKPSRV
