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CABYR_MOUSE
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   03-AUG-2022, entry version 145.
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.ENSMUSP00000111523; -.
DR   iPTMnet; Q9D424; -.
DR   PhosphoSitePlus; Q9D424; -.
DR   PaxDb; Q9D424; -.
DR   PRIDE; Q9D424; -.
DR   ProteomicsDB; 273875; -. [Q9D424-1]
DR   ProteomicsDB; 273876; -. [Q9D424-2]
DR   ProteomicsDB; 273877; -. [Q9D424-3]
DR   Antibodypedia; 22085; 93 antibodies from 24 providers.
DR   DNASU; 71132; -.
DR   Ensembl; ENSMUST00000080415; ENSMUSP00000079277; ENSMUSG00000024430. [Q9D424-1]
DR   Ensembl; ENSMUST00000115857; ENSMUSP00000111523; ENSMUSG00000024430. [Q9D424-1]
DR   Ensembl; ENSMUST00000119108; ENSMUSP00000113760; ENSMUSG00000024430. [Q9D424-3]
DR   Ensembl; ENSMUST00000121018; ENSMUSP00000113131; ENSMUSG00000024430. [Q9D424-2]
DR   Ensembl; ENSMUST00000150758; ENSMUSP00000118330; ENSMUSG00000024430. [Q9D424-1]
DR   Ensembl; ENSMUST00000186263; ENSMUSP00000140870; ENSMUSG00000024430. [Q9D424-1]
DR   Ensembl; ENSMUST00000191078; ENSMUSP00000140894; ENSMUSG00000024430. [Q9D424-1]
DR   Ensembl; ENSMUST00000234735; ENSMUSP00000157280; ENSMUSG00000024430. [Q9D424-2]
DR   GeneID; 71132; -.
DR   KEGG; mmu:71132; -.
DR   UCSC; uc008ecl.1; mouse. [Q9D424-3]
DR   UCSC; uc008ecm.1; mouse. [Q9D424-1]
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; PKMANPN; -.
DR   OrthoDB; 919811at2759; -.
DR   PhylomeDB; Q9D424; -.
DR   TreeFam; TF332959; -.
DR   BioGRID-ORCS; 71132; 1 hit in 74 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 55 other 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   InterPro; IPR038848; CABYR.
DR   InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR   PANTHER; PTHR15494; PTHR15494; 2.
DR   Pfam; PF02197; RIIa; 1.
DR   SMART; SM00394; RIIa; 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
 
 
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