ID CABYR_MOUSE Reviewed; 453 AA.
AC Q9D424; Q91Y41; Q91Y42;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 24-JAN-2024, entry version 153.
DE RecName: Full=Calcium-binding tyrosine phosphorylation-regulated protein;
DE AltName: Full=Calcium-binding protein 86;
DE AltName: Full=Testis-specific calcium-binding protein CBP86;
GN Name=Cabyr; Synonyms=Cbp86;
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] (ISOFORMS 1; 2 AND 3), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=12801634; DOI=10.1016/s0378-1119(03)00495-5;
RA Sen B., Mandal A., Wolkowicz M.J., Kim Y.-H., Reddi P.P., Shetty J.,
RA Bush L.A., Flickinger C.J., Herr J.C.;
RT "Splicing in murine CABYR and its genomic structure.";
RL Gene 310:67-78(2003).
RN [2]
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 [3]
RP INTERACTION WITH FSCB.
RX PubMed=17855365; DOI=10.1074/jbc.m702238200;
RA Li Y.-F., He W., Jha K.N., Klotz K., Kim Y.-H., Mandal A., Pulido S.,
RA Digilio L., Flickinger C.J., Herr J.C.;
RT "FSCB, a novel protein kinase A-phosphorylated calcium-binding protein, is
RT a CABYR-binding partner involved in late steps of fibrous sheath
RT biogenesis.";
RL J. Biol. Chem. 282:34104-34119(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May function as a regulator of both motility- and head-
CC associated functions such as capacitation and the acrosome reaction.
CC May bind calcium in vitro (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with FSCB. {ECO:0000269|PubMed:17855365}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12801634}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12801634}. Cell projection,
CC cilium, flagellum {ECO:0000269|PubMed:12801634}. Note=Localizes to
CC fibrous sheath including the surface of the longitudinal columns and
CC ribs of the principal piece of sperm flagella.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=CBP86-1, CBP86-6;
CC IsoId=Q9D424-1; Sequence=Displayed;
CC Name=2; Synonyms=CBP86-2;
CC IsoId=Q9D424-2; Sequence=VSP_016252, VSP_016255;
CC Name=3; Synonyms=CBP86-4;
CC IsoId=Q9D424-3; Sequence=VSP_016253, VSP_016254;
CC -!- TISSUE SPECIFICITY: Expressed in spermatozoa.
CC {ECO:0000269|PubMed:12801634}.
CC -!- PTM: Phosphorylated on tyrosine residues during in vitro capacitation.
CC Dephosphorylation affects its ability to bind calcium (By similarity).
CC {ECO:0000250}.
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DR EMBL; AF359382; AAK49987.1; -; mRNA.
DR EMBL; AF359383; AAK49988.1; -; mRNA.
DR EMBL; AF359384; AAK49989.1; -; mRNA.
DR EMBL; AF359385; AAK49990.1; -; mRNA.
DR EMBL; AK016856; BAB30467.1; -; mRNA.
DR CCDS; CCDS37739.1; -. [Q9D424-1]
DR CCDS; CCDS50223.1; -. [Q9D424-2]
DR CCDS; CCDS50224.1; -. [Q9D424-3]
DR RefSeq; NP_001035883.1; NM_001042418.1. [Q9D424-1]
DR RefSeq; NP_001035884.1; NM_001042419.1. [Q9D424-3]
DR RefSeq; NP_001035885.1; NM_001042420.1. [Q9D424-1]
DR RefSeq; NP_081963.1; NM_027687.2. [Q9D424-1]
DR RefSeq; NP_859420.2; NM_181731.3. [Q9D424-2]
DR RefSeq; XP_017173468.1; XM_017317979.1. [Q9D424-1]
DR AlphaFoldDB; Q9D424; -.
DR SMR; Q9D424; -.
DR BioGRID; 214495; 5.
DR STRING; 10090.ENSMUSP00000140870; -.
DR iPTMnet; Q9D424; -.
DR PhosphoSitePlus; Q9D424; -.
DR SwissPalm; Q9D424; -.
DR PaxDb; 10090-ENSMUSP00000111523; -.
DR ProteomicsDB; 273875; -. [Q9D424-1]
DR ProteomicsDB; 273876; -. [Q9D424-2]
DR ProteomicsDB; 273877; -. [Q9D424-3]
DR Antibodypedia; 22085; 101 antibodies from 24 providers.
DR DNASU; 71132; -.
DR Ensembl; ENSMUST00000080415.11; ENSMUSP00000079277.5; ENSMUSG00000024430.15. [Q9D424-1]
DR Ensembl; ENSMUST00000115857.9; ENSMUSP00000111523.3; ENSMUSG00000024430.15. [Q9D424-1]
DR Ensembl; ENSMUST00000119108.8; ENSMUSP00000113760.2; ENSMUSG00000024430.15. [Q9D424-3]
DR Ensembl; ENSMUST00000121018.8; ENSMUSP00000113131.2; ENSMUSG00000024430.15. [Q9D424-2]
DR Ensembl; ENSMUST00000150758.8; ENSMUSP00000118330.2; ENSMUSG00000024430.15. [Q9D424-1]
DR Ensembl; ENSMUST00000186263.2; ENSMUSP00000140870.2; ENSMUSG00000024430.15. [Q9D424-1]
DR Ensembl; ENSMUST00000191078.7; ENSMUSP00000140894.2; ENSMUSG00000024430.15. [Q9D424-1]
DR Ensembl; ENSMUST00000234735.2; ENSMUSP00000157280.2; ENSMUSG00000024430.15. [Q9D424-2]
DR GeneID; 71132; -.
DR KEGG; mmu:71132; -.
DR UCSC; uc008ecl.1; mouse. [Q9D424-3]
DR UCSC; uc008ecm.1; mouse. [Q9D424-1]
DR AGR; MGI:1918382; -.
DR CTD; 26256; -.
DR MGI; MGI:1918382; Cabyr.
DR VEuPathDB; HostDB:ENSMUSG00000024430; -.
DR eggNOG; ENOG502S1NF; Eukaryota.
DR GeneTree; ENSGT00390000000444; -.
DR HOGENOM; CLU_025626_0_0_1; -.
DR InParanoid; Q9D424; -.
DR OMA; QDWKPIP; -.
DR OrthoDB; 4011051at2759; -.
DR PhylomeDB; Q9D424; -.
DR TreeFam; TF332959; -.
DR BioGRID-ORCS; 71132; 1 hit in 79 CRISPR screens.
DR ChiTaRS; Cabyr; mouse.
DR PRO; PR:Q9D424; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9D424; Protein.
DR Bgee; ENSMUSG00000024430; Expressed in seminiferous tubule of testis and 57 other cell types or tissues.
DR ExpressionAtlas; Q9D424; baseline and differential.
DR Genevisible; Q9D424; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031514; C:motile cilium; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0097229; C:sperm end piece; IDA:MGI.
DR GO; GO:0035686; C:sperm fibrous sheath; IDA:BHF-UCL.
DR GO; GO:0097228; C:sperm principal piece; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISS:BHF-UCL.
DR GO; GO:0019904; F:protein domain specific binding; IPI:BHF-UCL.
DR GO; GO:0019722; P:calcium-mediated signaling; NAS:BHF-UCL.
DR GO; GO:0048240; P:sperm capacitation; NAS:BHF-UCL.
DR CDD; cd12100; DD_CABYR_SP17; 1.
DR Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR InterPro; IPR038848; CABYR.
DR InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR InterPro; IPR047579; DD_CABYR_SP17.
DR PANTHER; PTHR15494; CALCIUM-BINDING TYROSINE PHOSPHORYLATION-REGULATED PROTEIN; 1.
DR PANTHER; PTHR15494:SF0; CALCIUM-BINDING TYROSINE PHOSPHORYLATION-REGULATED PROTEIN; 1.
DR Pfam; PF02197; RIIa; 1.
DR SMART; SM00394; RIIa; 1.
DR SUPFAM; SSF47391; Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell projection; Cilium; Cytoplasm;
KW Cytoskeleton; Flagellum; Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..453
FT /note="Calcium-binding tyrosine phosphorylation-regulated
FT protein"
FT /id="PRO_0000089270"
FT DOMAIN 12..49
FT /note="RIIa"
FT REGION 86..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..165
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 183..381
FT /note="GNVPSTYSEVLMVDVATSTPAVPQDVLSAEFAEEVVLSAPLVCSGETVEVQV
FT VSKTSAQVVVGPVSEAEPPKASSAPLQGEQEPPAHEAPDTQVTSASRISSIYNDVPVNE
FT GVVYVEEIPGYIVIPFTDHDQVACVKEIEQSPPGSPKAVEPKTKISIESLKTVQVEENS
FT QHKSSVHVEAEATVLLSNTALDGQPEVPA -> ALATSEAGQPPPYSNMWTLYCLTDMN
FT QQSRPSPPPAPGPFPQATLYLPNPKEPQFLQNPPKVTSPTYVMMDDSKKTNAPPFILVG
FT SNVQEAQDWNPLPGHAVVSQAEALKRYAAVQVPIAVPADQTFQRPAPNPQNASPPTSGQ
FT DGPRPKSPVFLSVAFPVEDVAKKSSGSGDKRTPFGSYGIAGEITVTTAHVRRAEP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12801634"
FT /id="VSP_016252"
FT VAR_SEQ 183..220
FT /note="GNVPSTYSEVLMVDVATSTPAVPQDVLSAEFAEEVVLS -> EDVAKKSSGS
FT GDKRTPFGSYGIAGEITVTTAHVRRAEP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12801634"
FT /id="VSP_016253"
FT VAR_SEQ 221..453
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12801634"
FT /id="VSP_016254"
FT VAR_SEQ 382..453
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12801634"
FT /id="VSP_016255"
FT CONFLICT 17
FT /note="L -> P (in Ref. 1; AAK49988)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="F -> L (in Ref. 1; AAK49988)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 48333 MW; 7BCA9EB34D89F472 CRC64;
MISSKPRLVV PYGLKTLLEG VSRAILKTNP TNITQFAAVY FKELIVFREG NSSLDIKDLI
KQFHQMKVEK WAEGVTVEKK ECIKEPIKPP PVPCKPTHME KSTDTEEDNV AGPLFSNKTT
QFPSVHAEVQ SEETSEGARG PSDKPTTPKT DYTPPSSPPP APVSAEYAYV PADPAQFAAQ
MLGNVPSTYS EVLMVDVATS TPAVPQDVLS AEFAEEVVLS APLVCSGETV EVQVVSKTSA
QVVVGPVSEA EPPKASSAPL QGEQEPPAHE APDTQVTSAS RISSIYNDVP VNEGVVYVEE
IPGYIVIPFT DHDQVACVKE IEQSPPGSPK AVEPKTKISI ESLKTVQVEE NSQHKSSVHV
EAEATVLLSN TALDGQPEVP AEPLDAEGFF KVASENSLHL ETEIVIINPD DPGQEESGGN
AAPHSSGDPF PPAPGGLTEP EMQPDGEAAP EQV
//
