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EFHB_MOUSE
ID   EFHB_MOUSE              Reviewed;         853 AA.
AC   Q8CDU5; A2RSG9;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=EF-hand domain-containing family member B {ECO:0000305};
DE   AltName: Full=Cilia- and flagella-associated protein 21;
GN   Name=Efhb {ECO:0000312|MGI:MGI:3045296}; Synonyms=Cfap21;
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].
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].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Testis;
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   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: Cytosolic sensor for calcium, modulates the interaction of
CC       STIM1 and ORAI1 upon store depletion and the activation of store-
CC       operated Ca(2+) entry (SOCE) and NFAT translocation from cytosol to
CC       nucleus (By similarity). Microtubule inner protein (MIP) part of the
CC       dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is
CC       required for motile cilia beating (By similarity).
CC       {ECO:0000250|UniProtKB:F1MMV1, ECO:0000250|UniProtKB:Q8N7U6}.
CC   -!- SUBUNIT: Interacts with STIM1 and ORAI1; the interactions take place
CC       upon Ca(2+)-store depletion and dissociate through a Ca(2+)-dependent
CC       mechanism. Interaction with STIM1 inhibits STIM1 interaction with
CC       SARAF. {ECO:0000250|UniProtKB:Q8N7U6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N7U6}.
CC       Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:F1MMV1}.
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DR   EMBL; AK029550; BAC26511.1; -; mRNA.
DR   EMBL; CH466559; EDL23660.1; -; Genomic_DNA.
DR   EMBL; BC132103; AAI32104.1; -; mRNA.
DR   EMBL; BC137880; AAI37881.1; -; mRNA.
DR   CCDS; CCDS37652.1; -.
DR   RefSeq; NP_766085.2; NM_172497.3.
DR   AlphaFoldDB; Q8CDU5; -.
DR   SMR; Q8CDU5; -.
DR   STRING; 10090.ENSMUSP00000024725; -.
DR   iPTMnet; Q8CDU5; -.
DR   PhosphoSitePlus; Q8CDU5; -.
DR   MaxQB; Q8CDU5; -.
DR   PaxDb; Q8CDU5; -.
DR   PRIDE; Q8CDU5; -.
DR   ProteomicsDB; 275439; -.
DR   Antibodypedia; 27043; 109 antibodies from 17 providers.
DR   DNASU; 211482; -.
DR   Ensembl; ENSMUST00000024725; ENSMUSP00000024725; ENSMUSG00000023931.
DR   GeneID; 211482; -.
DR   KEGG; mmu:211482; -.
DR   UCSC; uc008czl.1; mouse.
DR   CTD; 151651; -.
DR   MGI; MGI:3045296; Efhb.
DR   VEuPathDB; HostDB:ENSMUSG00000023931; -.
DR   eggNOG; ENOG502QV2M; Eukaryota.
DR   GeneTree; ENSGT00530000063528; -.
DR   HOGENOM; CLU_017580_0_0_1; -.
DR   InParanoid; Q8CDU5; -.
DR   OMA; WAPLGKS; -.
DR   OrthoDB; 1016066at2759; -.
DR   PhylomeDB; Q8CDU5; -.
DR   TreeFam; TF323832; -.
DR   BioGRID-ORCS; 211482; 0 hits in 71 CRISPR screens.
DR   ChiTaRS; Efhb; mouse.
DR   PRO; PR:Q8CDU5; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q8CDU5; protein.
DR   Bgee; ENSMUSG00000023931; Expressed in spermatid and 56 other tissues.
DR   ExpressionAtlas; Q8CDU5; baseline and differential.
DR   Genevisible; Q8CDU5; MM.
DR   GO; GO:0005879; C:axonemal microtubule; ISS:UniProtKB.
DR   GO; GO:0061891; F:calcium ion sensor activity; ISS:UniProtKB.
DR   GO; GO:0032091; P:negative regulation of protein binding; ISS:UniProtKB.
DR   GO; GO:0070884; P:regulation of calcineurin-NFAT signaling cascade; ISS:UniProtKB.
DR   GO; GO:2001256; P:regulation of store-operated calcium entry; ISS:UniProtKB.
DR   CDD; cd00051; EFh; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR040193; EFHC1/EFHC2/EFHB.
DR   PANTHER; PTHR12086; PTHR12086; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   1: Evidence at protein level;
KW   Calcium; Cell projection; Cytoplasm; Cytoskeleton; Metal-binding;
KW   Reference proteome; Repeat.
FT   CHAIN           1..853
FT                   /note="EF-hand domain-containing family member B"
FT                   /id="PRO_0000252095"
FT   DOMAIN          581..616
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          617..652
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         594
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         598
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         605
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         630
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         632
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         634
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         641
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   CONFLICT        632
FT                   /note="D -> G (in Ref. 1; BAC26511)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   853 AA;  95743 MW;  9051B1D2F35AA68E CRC64;
     MCSFVRVGSP KPLQTSASPL EMSSLRRTRA PEISELGLTP EQKDDIRDRV LRGSKSPTEL
     GFDLRLEQDR KWRERMGSSE AKSPPCHALG VGLERHTISG TPTEMGNLGL HKGSAFQGSK
     PLGVLPGRVG PENKGLPPRL RYGGTLHPPF STVHASPLAA ESRRRPLAWG SAWTDAVVEK
     QPVVGLELRK EPEKEPTCVV MNPYPEMPPK EVDIGLPQTQ ESDEAKNTEP LIGLVREPSE
     CPFAQQPEEK KEPGSTEPGV EPPGNIRPIY SGKFFDRVPC WPSAGKVKPV GYRVATCLTE
     KLPRLMTPPE AKKYFNFRYP PAGAERVFYG RANDPQIAPY LTHGLRSKIS IPMGSLINPQ
     PITTFQQKIK DKKESIYFSH QRAPLGKSHD QTPGLPKGMD VINTTLGTPT IRELSVRDTV
     NPSKSFEDVL KEGQEGHDLY TVSHNDYFAG EAKNRKYNPA SFHRFNLYGI PTPHFNDGRT
     MAKALHWLHE LQMERGAKIV SKRVDDFKEK FQHKLGKVLD PIAETMNVPP GHTFGSCLHP
     EEYGAGDLIH YRSPDEYLRG KDHQRAVVAA ARHHLKKFNH QNFDTLQVAF RHYDKKGDGV
     IDRAELHEAC VQANLHLDKM LLDHLFDYCD VDQDGLINYL EFANFLNWKD RIPLKEHEKR
     VVVKGKKPDC ENVTDTSMGE AEPSLLINPE DIVPKEPGSS EETLRTIQRP GDKVSHQYKT
     TSSEINAVVG AVPSMCHPIF GVPTIRSDIS APRIRRVSDM NNYGDEGNAY SLLHPSIFSQ
     KGVFERDFFK TRSKEEISDI LTNIGVKLSK EEFENVWNLA SKKHQRGEVC VETIRNVLDE
     LLHADLVKCK TAM
 
 
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