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Calcium-binding tyrosine phosphorylation-regulated protein (Calcium-binding protein 86) (Testis-specific calcium-binding protein CBP86)

 CABYR_MOUSE             Reviewed;         453 AA.
Q9D424; Q91Y41; Q91Y42;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
12-SEP-2018, entry version 125.
RecName: Full=Calcium-binding tyrosine phosphorylation-regulated protein;
AltName: Full=Calcium-binding protein 86;
AltName: Full=Testis-specific calcium-binding protein CBP86;
Name=Cabyr; Synonyms=Cbp86;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Testis;
PubMed=12801634; DOI=10.1016/S0378-1119(03)00495-5;
Sen B., Mandal A., Wolkowicz M.J., Kim Y.-H., Reddi P.P., Shetty J.,
Bush L.A., Flickinger C.J., Herr J.C.;
"Splicing in murine CABYR and its genomic structure.";
Gene 310:67-78(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
INTERACTION WITH FSCB.
PubMed=17855365; DOI=10.1074/jbc.M702238200;
Li Y.-F., He W., Jha K.N., Klotz K., Kim Y.-H., Mandal A., Pulido S.,
Digilio L., Flickinger C.J., Herr J.C.;
"FSCB, a novel protein kinase A-phosphorylated calcium-binding
protein, is a CABYR-binding partner involved in late steps of fibrous
sheath biogenesis.";
J. Biol. Chem. 282:34104-34119(2007).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: May function as a regulator of both motility- and head-
associated functions such as capacitation and the acrosome
reaction. May bind calcium in vitro (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Interacts with FSCB. {ECO:0000269|PubMed:17855365}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12801634}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12801634}. Cell
projection, cilium, flagellum {ECO:0000269|PubMed:12801634}.
Note=Localizes to fibrous sheath including the surface of the
longitudinal columns and ribs of the principal piece of sperm
flagella.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=CBP86-1, CBP86-6;
IsoId=Q9D424-1; Sequence=Displayed;
Name=2; Synonyms=CBP86-2;
IsoId=Q9D424-2; Sequence=VSP_016252, VSP_016255;
Name=3; Synonyms=CBP86-4;
IsoId=Q9D424-3; Sequence=VSP_016253, VSP_016254;
-!- TISSUE SPECIFICITY: Expressed in spermatozoa.
{ECO:0000269|PubMed:12801634}.
-!- PTM: Phosphorylated on tyrosine residues during in vitro
capacitation. Dephosphorylation affects its ability to bind
calcium (By similarity). {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; AF359382; AAK49987.1; -; mRNA.
EMBL; AF359383; AAK49988.1; -; mRNA.
EMBL; AF359384; AAK49989.1; -; mRNA.
EMBL; AF359385; AAK49990.1; -; mRNA.
EMBL; AK016856; BAB30467.1; -; mRNA.
CCDS; CCDS37739.1; -. [Q9D424-1]
CCDS; CCDS50223.1; -. [Q9D424-2]
CCDS; CCDS50224.1; -. [Q9D424-3]
RefSeq; NP_001035883.1; NM_001042418.1. [Q9D424-1]
RefSeq; NP_001035884.1; NM_001042419.1. [Q9D424-3]
RefSeq; NP_001035885.1; NM_001042420.1. [Q9D424-1]
RefSeq; NP_081963.1; NM_027687.2. [Q9D424-1]
RefSeq; NP_859420.2; NM_181731.3. [Q9D424-2]
RefSeq; XP_017173468.1; XM_017317979.1. [Q9D424-1]
UniGene; Mm.179740; -.
ProteinModelPortal; Q9D424; -.
SMR; Q9D424; -.
BioGrid; 214495; 5.
STRING; 10090.ENSMUSP00000079277; -.
iPTMnet; Q9D424; -.
PhosphoSitePlus; Q9D424; -.
PaxDb; Q9D424; -.
PRIDE; Q9D424; -.
Ensembl; ENSMUST00000080415; ENSMUSP00000079277; ENSMUSG00000024430. [Q9D424-1]
Ensembl; ENSMUST00000115857; ENSMUSP00000111523; ENSMUSG00000024430. [Q9D424-1]
Ensembl; ENSMUST00000119108; ENSMUSP00000113760; ENSMUSG00000024430. [Q9D424-3]
Ensembl; ENSMUST00000121018; ENSMUSP00000113131; ENSMUSG00000024430. [Q9D424-2]
Ensembl; ENSMUST00000150758; ENSMUSP00000118330; ENSMUSG00000024430. [Q9D424-1]
Ensembl; ENSMUST00000186263; ENSMUSP00000140870; ENSMUSG00000024430. [Q9D424-1]
Ensembl; ENSMUST00000191078; ENSMUSP00000140894; ENSMUSG00000024430. [Q9D424-1]
GeneID; 71132; -.
KEGG; mmu:71132; -.
UCSC; uc008ecl.1; mouse. [Q9D424-3]
UCSC; uc008ecm.1; mouse. [Q9D424-1]
CTD; 26256; -.
MGI; MGI:1918382; Cabyr.
eggNOG; ENOG410IFPT; Eukaryota.
eggNOG; ENOG410ZQAQ; LUCA.
GeneTree; ENSGT00390000000444; -.
HOGENOM; HOG000059568; -.
HOVERGEN; HBG080982; -.
InParanoid; Q9D424; -.
OMA; EQIVIPF; -.
OrthoDB; EOG091G18VB; -.
PhylomeDB; Q9D424; -.
TreeFam; TF332959; -.
ChiTaRS; Cabyr; mouse.
PRO; PR:Q9D424; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000024430; Expressed in 51 organ(s), highest expression level in testis.
ExpressionAtlas; Q9D424; baseline and differential.
Genevisible; Q9D424; MM.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0031514; C:motile cilium; IDA:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0097229; C:sperm end piece; IDA:MGI.
GO; GO:0035686; C:sperm fibrous sheath; IDA:BHF-UCL.
GO; GO:0097228; C:sperm principal piece; IDA:MGI.
GO; GO:0005509; F:calcium ion binding; IDA:MGI.
GO; GO:0019899; F:enzyme binding; ISS:BHF-UCL.
GO; GO:0019904; F:protein domain specific binding; IPI:BHF-UCL.
GO; GO:0046982; F:protein heterodimerization activity; IDA:BHF-UCL.
GO; GO:0019722; P:calcium-mediated signaling; NAS:BHF-UCL.
GO; GO:0051259; P:protein complex oligomerization; NAS:BHF-UCL.
GO; GO:0048240; P:sperm capacitation; NAS:BHF-UCL.
InterPro; IPR038848; CABYR.
InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
PANTHER; PTHR15494; PTHR15494; 1.
Pfam; PF02197; RIIa; 1.
SMART; SM00394; RIIa; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Cell projection; Cilium;
Complete proteome; Cytoplasm; Cytoskeleton; Flagellum; Metal-binding;
Phosphoprotein; Reference proteome.
CHAIN 1 453 Calcium-binding tyrosine phosphorylation-
regulated protein.
/FTId=PRO_0000089270.
DOMAIN 12 49 RIIa.
VAR_SEQ 183 381 GNVPSTYSEVLMVDVATSTPAVPQDVLSAEFAEEVVLSAPL
VCSGETVEVQVVSKTSAQVVVGPVSEAEPPKASSAPLQGEQ
EPPAHEAPDTQVTSASRISSIYNDVPVNEGVVYVEEIPGYI
VIPFTDHDQVACVKEIEQSPPGSPKAVEPKTKISIESLKTV
QVEENSQHKSSVHVEAEATVLLSNTALDGQPEVPA -> AL
ATSEAGQPPPYSNMWTLYCLTDMNQQSRPSPPPAPGPFPQA
TLYLPNPKEPQFLQNPPKVTSPTYVMMDDSKKTNAPPFILV
GSNVQEAQDWNPLPGHAVVSQAEALKRYAAVQVPIAVPADQ
TFQRPAPNPQNASPPTSGQDGPRPKSPVFLSVAFPVEDVAK
KSSGSGDKRTPFGSYGIAGEITVTTAHVRRAEP (in
isoform 2).
{ECO:0000303|PubMed:12801634}.
/FTId=VSP_016252.
VAR_SEQ 183 220 GNVPSTYSEVLMVDVATSTPAVPQDVLSAEFAEEVVLS ->
EDVAKKSSGSGDKRTPFGSYGIAGEITVTTAHVRRAEP
(in isoform 3).
{ECO:0000303|PubMed:12801634}.
/FTId=VSP_016253.
VAR_SEQ 221 453 Missing (in isoform 3).
{ECO:0000303|PubMed:12801634}.
/FTId=VSP_016254.
VAR_SEQ 382 453 Missing (in isoform 2).
{ECO:0000303|PubMed:12801634}.
/FTId=VSP_016255.
CONFLICT 17 17 L -> P (in Ref. 1; AAK49988).
{ECO:0000305}.
CONFLICT 41 41 F -> L (in Ref. 1; AAK49988).
{ECO:0000305}.
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


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