EFCB7_MOUSE
ID EFCB7_MOUSE Reviewed; 628 AA.
AC Q8VDY4; Q3UQS0; Q5DTU8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=EF-hand calcium-binding domain-containing protein 7;
GN Name=Efcab7; Synonyms=Kiaa1799;
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 TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart;
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 MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 FUNCTION, IDENTIFICATION IN THE EVC COMPLEX, INTERACTION WITH EVC; EVC2 AND
RP IQCE, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=24582806; DOI=10.1016/j.devcel.2014.01.021;
RA Pusapati G.V., Hughes C.E., Dorn K.V., Zhang D., Sugianto P., Aravind L.,
RA Rohatgi R.;
RT "EFCAB7 and IQCE regulate hedgehog signaling by tethering the EVC-EVC2
RT complex to the base of primary cilia.";
RL Dev. Cell 28:483-496(2014).
CC -!- FUNCTION: Component of the EvC complex that positively regulates
CC ciliary Hedgehog (Hh) signaling (PubMed:24582806). Required for the
CC localization of the EVC2:EVC subcomplex at the base of primary cilia
CC (PubMed:24582806). {ECO:0000269|PubMed:24582806}.
CC -!- SUBUNIT: Component of the EvC complex composed of EFCAB7, IQCE, EVC2
CC and EVC; built from two subcomplexes, EVC2:EVC and EFCAB7:IQCE
CC (PubMed:24582806). Interacts (via EF-hand 1 and 2) with IQCE (via N-
CC terminus); this interaction anchors the EVC-EVC2 complex in a signaling
CC microdomain at the base of cilia and stimulates the Hedgehog (Hh)
CC pathway (PubMed:24582806). Interacts with EVC2 (via N-terminal end)
CC (PubMed:24582806). Interacts with EVC (PubMed:24582806).
CC {ECO:0000269|PubMed:24582806}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC {ECO:0000269|PubMed:24582806}; Peripheral membrane protein
CC {ECO:0000269|PubMed:24582806}; Cytoplasmic side
CC {ECO:0000269|PubMed:24582806}. Note=The EvC complex localizes at the
CC base of cilia in the EvC zone of primary cilia in a EFCAB7-dependent
CC manner (PubMed:24582806). {ECO:0000269|PubMed:24582806}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90467.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE24969.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK220422; BAD90467.1; ALT_INIT; mRNA.
DR EMBL; AK142188; BAE24969.1; ALT_INIT; mRNA.
DR EMBL; BC020077; AAH20077.1; -; mRNA.
DR RefSeq; NP_663524.1; NM_145549.1.
DR AlphaFoldDB; Q8VDY4; -.
DR SMR; Q8VDY4; -.
DR iPTMnet; Q8VDY4; -.
DR PhosphoSitePlus; Q8VDY4; -.
DR EPD; Q8VDY4; -.
DR MaxQB; Q8VDY4; -.
DR PaxDb; Q8VDY4; -.
DR PRIDE; Q8VDY4; -.
DR ProteomicsDB; 277728; -.
DR Antibodypedia; 33354; 119 antibodies from 20 providers.
DR Ensembl; ENSMUST00000136874; ENSMUSP00000118989; ENSMUSG00000073791.
DR Ensembl; ENSMUST00000239516; ENSMUSP00000159398; ENSMUSG00000073791.
DR GeneID; 230500; -.
DR KEGG; mmu:230500; -.
DR UCSC; uc008tuz.1; mouse.
DR CTD; 84455; -.
DR MGI; MGI:2385199; Efcab7.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00390000015466; -.
DR InParanoid; Q8VDY4; -.
DR OMA; TVCITIK; -.
DR OrthoDB; 1059411at2759; -.
DR PhylomeDB; Q8VDY4; -.
DR BioGRID-ORCS; 230500; 1 hit in 51 CRISPR screens.
DR PRO; PR:Q8VDY4; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8VDY4; protein.
DR Bgee; ENSMUSG00000073791; Expressed in spermatocyte and 64 other tissues.
DR ExpressionAtlas; Q8VDY4; baseline and differential.
DR GO; GO:0060170; C:ciliary membrane; IDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0098797; C:plasma membrane protein complex; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:UniProtKB.
DR GO; GO:1903569; P:positive regulation of protein localization to ciliary membrane; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP: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 Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Cell projection; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..628
FT /note="EF-hand calcium-binding domain-containing protein 7"
FT /id="PRO_0000317267"
FT DOMAIN 102..137
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 138..173
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 402..437
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 415
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 426
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A8K855"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A8K855"
FT CONFLICT 410
FT /note="I -> L (in Ref. 1; BAD90467)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="A -> R (in Ref. 1; BAD90467)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 628 AA; 71442 MW; 856BBED585598B67 CRC64;
MASNPGSDAA LGTQNPLLSG SPRTKKFPLT EQEVFYMNCR AAYLTIFKSS LENIISKDQL
YLALQHAGRN PSQKTINKYW TPQTAKLNFD DFCIILSKEK PTSKAELLKS FKKLDVNDDG
AILHSDLQKY LTKRGEKMTQ EEVNAVINLA DINANGKFDY VKFCKLYMTT SEQCLKTTLE
RLEADSKLRR QQFGSHMEGS PERGPSPAPK PSPRVIRKND QETFSSKGDT SHALLSTTRK
FKTSVSFTMT MSANSNQDST LTEPNLKDWQ CAQSKGCFFL EEDGEVVSHQ YKMHIAQRSV
LYLTIKPLYL SQVEGKRCPW LSVDTALYIL KKNENPAEPQ LMCFTELRNR EVFGWTGELE
AGIYWLIPST TGCRLKKETK PVTEEAQLVH RDETGELSLT SEFRSTLSEI FEVIDLDGNG
LISLEEYNFF ELRTSGEKCD EDAWAVCREN FDTKKNELTR QGFMDLHLME ANDREGDPLD
LWVTLHSMGY NKALELTEAC PFVINIYAER CKPRIKVVHM EACSGQLEKA ICKSVLDRSD
AKVMDGYENI IVHTCNYDTW ITSIIENKSD NKVIIHINNE LSKNCVNNRG LNIFAVEVAP
RSTMVCQHVM PLNEQEEWIY CCVYSLVA
