EFCB7_HUMAN
ID EFCB7_HUMAN Reviewed; 629 AA.
AC A8K855; Q658P0; Q96B95; Q96JM6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=EF-hand calcium-binding domain-containing protein 7;
GN Name=EFCAB7; Synonyms=KIAA1799;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Esophagus, and Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ILE-248;
RP THR-262 AND LYS-375.
RC TISSUE=Skin;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 353-629, AND VARIANT LYS-375.
RC TISSUE=Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200 AND SER-212, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Component of the EvC complex that positively regulates
CC ciliary Hedgehog (Hh) signaling. Required for the localization of the
CC EVC2:EVC subcomplex at the base of primary cilia.
CC {ECO:0000250|UniProtKB:Q8VDY4}.
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 Interacts (via EF-hand 1 and 2) with IQCE (via N-terminus); this
CC interaction anchors the EVC-EVC2 complex in a signaling microdomain at
CC the base of cilia and stimulates the Hedgehog (Hh) pathway. Interacts
CC with EVC2 (via N-terminal end). Interacts with EVC.
CC {ECO:0000250|UniProtKB:Q8VDY4}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC {ECO:0000250|UniProtKB:Q8VDY4}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8VDY4}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q8VDY4}. Note=The EvC complex localizes at the
CC base of cilia in the EvC zone of primary cilia in a EFCAB7-dependent
CC manner. {ECO:0000250|UniProtKB:Q8VDY4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A8K855-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A8K855-2; Sequence=VSP_030930;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB47428.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB058702; BAB47428.1; ALT_INIT; mRNA.
DR EMBL; AK292220; BAF84909.1; -; mRNA.
DR EMBL; AK315850; BAF98741.1; -; mRNA.
DR EMBL; AL109925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX004807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06570.1; -; Genomic_DNA.
DR EMBL; BC015814; AAH15814.1; -; mRNA.
DR EMBL; AL833720; CAH56237.1; -; mRNA.
DR CCDS; CCDS30737.1; -. [A8K855-1]
DR RefSeq; NP_115813.2; NM_032437.3. [A8K855-1]
DR RefSeq; XP_005271331.1; XM_005271274.3. [A8K855-2]
DR RefSeq; XP_006711040.1; XM_006710977.1. [A8K855-1]
DR AlphaFoldDB; A8K855; -.
DR SMR; A8K855; -.
DR BioGRID; 124090; 14.
DR IntAct; A8K855; 10.
DR STRING; 9606.ENSP00000360129; -.
DR iPTMnet; A8K855; -.
DR PhosphoSitePlus; A8K855; -.
DR BioMuta; EFCAB7; -.
DR EPD; A8K855; -.
DR jPOST; A8K855; -.
DR MassIVE; A8K855; -.
DR MaxQB; A8K855; -.
DR PaxDb; A8K855; -.
DR PeptideAtlas; A8K855; -.
DR PRIDE; A8K855; -.
DR ProteomicsDB; 1875; -. [A8K855-1]
DR ProteomicsDB; 1876; -. [A8K855-2]
DR Antibodypedia; 33354; 119 antibodies from 20 providers.
DR DNASU; 84455; -.
DR Ensembl; ENST00000371088.5; ENSP00000360129.4; ENSG00000203965.13. [A8K855-1]
DR GeneID; 84455; -.
DR KEGG; hsa:84455; -.
DR MANE-Select; ENST00000371088.5; ENSP00000360129.4; NM_032437.4; NP_115813.2.
DR UCSC; uc001dbf.4; human. [A8K855-1]
DR CTD; 84455; -.
DR DisGeNET; 84455; -.
DR GeneCards; EFCAB7; -.
DR HGNC; HGNC:29379; EFCAB7.
DR HPA; ENSG00000203965; Low tissue specificity.
DR MIM; 617632; gene.
DR neXtProt; NX_A8K855; -.
DR OpenTargets; ENSG00000203965; -.
DR PharmGKB; PA162384389; -.
DR VEuPathDB; HostDB:ENSG00000203965; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00390000015466; -.
DR HOGENOM; CLU_031520_1_0_1; -.
DR InParanoid; A8K855; -.
DR OMA; TVCITIK; -.
DR OrthoDB; 1059411at2759; -.
DR PhylomeDB; A8K855; -.
DR TreeFam; TF329354; -.
DR PathwayCommons; A8K855; -.
DR Reactome; R-HSA-5635838; Activation of SMO.
DR SignaLink; A8K855; -.
DR BioGRID-ORCS; 84455; 11 hits in 1078 CRISPR screens.
DR ChiTaRS; EFCAB7; human.
DR GenomeRNAi; 84455; -.
DR Pharos; A8K855; Tdark.
DR PRO; PR:A8K855; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; A8K855; protein.
DR Bgee; ENSG00000203965; Expressed in oocyte and 177 other tissues.
DR Genevisible; A8K855; HS.
DR GO; GO:0060170; C:ciliary membrane; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; TAS:Reactome.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0098797; C:plasma membrane protein complex; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
DR GO; GO:1903569; P:positive regulation of protein localization to ciliary membrane; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; 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 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 Alternative splicing; Calcium; Cell membrane; Cell projection; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..629
FT /note="EF-hand calcium-binding domain-containing protein 7"
FT /id="PRO_0000317266"
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 403..438
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 418
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 420
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 427
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:0007744|PubMed:23186163"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 606..629
FT /note="VCQHVMPLNERQEWIYYCIYSLIS -> P (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11347906"
FT /id="VSP_030930"
FT VARIANT 27
FT /note="F -> I (in dbSNP:rs17125106)"
FT /id="VAR_038493"
FT VARIANT 186
FT /note="S -> G (in dbSNP:rs9436246)"
FT /id="VAR_038494"
FT VARIANT 248
FT /note="T -> I (in dbSNP:rs6693255)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038495"
FT VARIANT 262
FT /note="M -> T (in dbSNP:rs6657480)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038496"
FT VARIANT 375
FT /note="R -> K (in dbSNP:rs2273367)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_038497"
SQ SEQUENCE 629 AA; 71981 MW; 0C91918C36D7E0B8 CRC64;
MAISPRSDAT FSSQKSTPSE SPRTKKFPLT EEEIFYMNCR AAYLTVFKSS LENIISKDQL
YLALQHAGRN PSQKTINKYW TPQTAKLNFD DFCIILRKEK PTSKAELLKS FKQLDVNDDG
CILHTDLYKF LTKRGEKMTR EEVNAIINLA DVNADGKFDY IKFCKLYMTT NEQCLKTTLE
KLEVDSKLMR HQFGNHIEGS PERDPSPVPK PSPKITRKTD PETFLNKGDT RSSLLSATRK
FKTSVSFTVT MGANGNRNSK LMEPNLIKDW QHMQSKGCFF LEEDGEIISH QYRMQIAQRS
MVYLTIKPLN LSQVEGKPSP WLSVDTALYI LKENESQANL QLVCFTELRN REVFGWTGEL
GPGIYWLIPS TTGCRLRKKI KPVTDEAQLV YRDETGELFL TKEFKSTLSD IFEVIDLDGN
GLLSLEEYNF FELRTSGEKC DEDAWAVCRE NFDTKRNELT RQGFMDLNLM EANDREGDPC
DLWVTLHSMG YNKALELTEA CPFVIDIYAE KCKPKIKAVH MEACSGQLEK AICKSVLSNG
DAKVMDGYEN IIVHTYSCDT WITSVIENKS DEKVIIHISN ELSKNCINNR GLNIFAVEVG
PKSTMVCQHV MPLNERQEWI YYCIYSLIS
