EVC_MOUSE
ID EVC_MOUSE Reviewed; 1005 AA.
AC P57680; E9QPK2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=EvC complex member EVC {ECO:0000305};
DE AltName: Full=Ellis-van Creveld syndrome protein homolog;
GN Name=Evc;
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], AND ALTERNATIVE SPLICING.
RC TISSUE=Brain;
RX PubMed=10700184; DOI=10.1038/73508;
RA Ruiz-Perez V.L., Ide S.E., Strom T.M., Lorenz B., Wilson D., Woods K.,
RA King L., Francomano C., Freisinger P., Spranger S., Marino B.,
RA Dallapiccola B., Wright M., Meitinger T., Polymeropoulos M.H., Goodship J.;
RT "Mutations in a new gene in Ellis-van Creveld syndrome and Weyers
RT acrodental dysostosis.";
RL Nat. Genet. 24:283-286(2000).
RN [2]
RP ERRATUM OF PUBMED:10700184.
RA Ruiz-Perez V.L., Ide S.E., Strom T.M., Lorenz B., Wilson D., Woods K.,
RA King L., Francomano C., Freisinger P., Spranger S., Marino B.,
RA Dallapiccola B., Wright M., Meitinger T., Polymeropoulos M.H., Goodship J.;
RL Nat. Genet. 25:125-125(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=17660199; DOI=10.1242/dev.007542;
RA Ruiz-Perez V.L., Blair H.J., Rodriguez-Andres M.E., Blanco M.J., Wilson A.,
RA Liu Y.N., Miles C., Peters H., Goodship J.A.;
RT "Evc is a positive mediator of Ihh-regulated bone growth that localises at
RT the base of chondrocyte cilia.";
RL Development 134:2903-2912(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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).
RN [6]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND INTERACTION WITH EVC2.
RX PubMed=21356043; DOI=10.1186/1741-7007-9-14;
RA Blair H.J., Tompson S., Liu Y.N., Campbell J., MacArthur K., Ponting C.P.,
RA Ruiz-Perez V.L., Goodship J.A.;
RT "Evc2 is a positive modulator of Hedgehog signalling that interacts with
RT Evc at the cilia membrane and is also found in the nucleus.";
RL BMC Biol. 9:14-14(2011).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE EVC COMPLEX, INTERACTION WITH EFCAB7; EVC2
RP AND 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:17660199, PubMed:24582806).
CC Involved in endochondral growth and skeletal development
CC (PubMed:17660199). {ECO:0000269|PubMed:17660199,
CC 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 with EVC2 (PubMed:24582806,
CC PubMed:21356043). Interacts with EFCAB7 (PubMed:24582806). Interacts
CC with IQCE (PubMed:24582806). {ECO:0000269|PubMed:24582806}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21356043};
CC Single-pass membrane protein {ECO:0000269|PubMed:21356043}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:17660199}. Cell
CC projection, cilium {ECO:0000269|PubMed:21356043}. Cell projection,
CC cilium membrane {ECO:0000269|PubMed:21356043,
CC ECO:0000269|PubMed:24582806}. Note=EVC2 is required for the
CC localization of EVC at the base of primary cilia (PubMed:21356043). The
CC EvC complex localizes at the base of cilia in the EvC zone of primary
CC cilia in a EFCAB7-dependent manner (PubMed:24582806).
CC {ECO:0000269|PubMed:21356043, ECO:0000269|PubMed:24582806}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P57680-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P57680-2; Sequence=VSP_004247;
CC -!- TISSUE SPECIFICITY: Expressed in the developing skeleton and the
CC orofacial region. Expression is general to all the cartilaginous
CC components of the skeleton, including the chondrocranium, the
CC vertebrae, the rib cage, and the axial skeleton by 15.5 dpc.
CC {ECO:0000269|PubMed:17660199}.
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DR EMBL; AJ250841; CAB76567.1; -; mRNA.
DR EMBL; AJ250841; CAB76568.1; ALT_SEQ; mRNA.
DR EMBL; AC111129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS19247.1; -. [P57680-1]
DR RefSeq; NP_067267.2; NM_021292.2. [P57680-1]
DR RefSeq; XP_006504105.1; XM_006504042.3. [P57680-2]
DR AlphaFoldDB; P57680; -.
DR SMR; P57680; -.
DR STRING; 10090.ENSMUSP00000031005; -.
DR PhosphoSitePlus; P57680; -.
DR MaxQB; P57680; -.
DR PaxDb; P57680; -.
DR PRIDE; P57680; -.
DR ProteomicsDB; 275900; -. [P57680-1]
DR ProteomicsDB; 275901; -. [P57680-2]
DR Antibodypedia; 2233; 96 antibodies from 15 providers.
DR DNASU; 59056; -.
DR Ensembl; ENSMUST00000031005; ENSMUSP00000031005; ENSMUSG00000029122. [P57680-1]
DR GeneID; 59056; -.
DR KEGG; mmu:59056; -.
DR UCSC; uc008xfo.2; mouse. [P57680-1]
DR CTD; 2121; -.
DR MGI; MGI:1890596; Evc.
DR VEuPathDB; HostDB:ENSMUSG00000029122; -.
DR eggNOG; ENOG502QUDD; Eukaryota.
DR GeneTree; ENSGT00940000154127; -.
DR HOGENOM; CLU_014037_0_0_1; -.
DR InParanoid; P57680; -.
DR OMA; QMRMSRK; -.
DR OrthoDB; 133009at2759; -.
DR TreeFam; TF335835; -.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR BioGRID-ORCS; 59056; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Evc; mouse.
DR PRO; PR:P57680; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P57680; protein.
DR Bgee; ENSMUSG00000029122; Expressed in right kidney and 195 other tissues.
DR ExpressionAtlas; P57680; baseline and differential.
DR Genevisible; P57680; MM.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0060170; C:ciliary membrane; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0098797; C:plasma membrane protein complex; IDA:UniProtKB.
DR GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR GO; GO:0003416; P:endochondral bone growth; IMP:UniProtKB.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:UniProtKB.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:InterPro.
DR InterPro; IPR026582; Evc.
DR InterPro; IPR026501; Limbin/Ellis-van_Creveld.
DR PANTHER; PTHR16795; PTHR16795; 1.
DR PANTHER; PTHR16795:SF13; PTHR16795:SF13; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cilium; Cytoplasm;
KW Cytoskeleton; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1005
FT /note="EvC complex member EVC"
FT /id="PRO_0000087103"
FT TOPO_DOM 1..21
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..1005
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 58..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..952
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 966..978
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_004247"
FT CONFLICT 376
FT /note="S -> A (in Ref. 1; CAB76567)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="T -> M (in Ref. 1; CAB76567)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="F -> L (in Ref. 1; CAB76567)"
FT /evidence="ECO:0000305"
FT CONFLICT 902
FT /note="L -> F (in Ref. 1; CAB76567)"
FT /evidence="ECO:0000305"
FT CONFLICT 923
FT /note="K -> N (in Ref. 1; CAB76567)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1005 AA; 113003 MW; 8BA872BE7D5822DB CRC64;
MTCTKDARLQ LGREALQAAP TLLVPAVLLG GVLGLGLGLW LGCRASHLRA RLQKDDRKRL
LGSSEPPAQS LRDTGSQAKA RRRQRETTRD EDAPEVCEPS LSGNITAFAL KARVVYPINQ
KFRPLADGSS HPSLHENLTQ AAAILPHLPH QPAEASPASS LGSLSQAGKE DGSSSSSMRS
TYSDDRILQC AFLRVGSFPE ILACESVDID LCVCSLHLKD LLQVDTALRQ EKHLMFIQIL
KACLLDFFPK KKPDDELCQK VLSKQEHDLE ELEKGLQARL ANTEMLGTGD SGYVSLADVE
RKERELSEQL IDNMGAFWKQ MESIQPTLMD QFKCSSSKAR QFMMTLTGRM IVAEGLLHDS
QDLHVLDTLE RTMGRSHLAR MVEFLRTQIQ EETKCRLAAI SRGLELLTVQ GQLSGRQKEE
LLTQQHKAFW EEAERFGREF TQRGKDLVQA SQARQAEAAA ELTQTQEEER RSFLADSQLT
SDPGEFLKAF HEVLERQRLT RSDQEGDEDT RITEAMAALC QELYCSTMGT FQKFVDSLFL
KTLPEVTSLP VAECETLRQQ VQEQAARQLG QADRFRRRQW GLLCDLLEQD KRVWLEEGTL
STVLQRQLRD HHESTIHGVL SRFSGLSEES SRGILQGHEL LLCSALRRLA LRGTTITALA
QMRLSGKKRL LQELHEQLAL EQGVSPCLEE HQWQLLRALE ARIQEEAARL EDEAQQTGLR
LQQQLLAEAQ EAGRLLQLHM ERVIGQALLV HARNVASKGR TREKEDFKRT LVETVVESVY
VTSTSVNRLV QAHYQAVGKL LQAHEEQLLQ RLKTLQGERI NAYKLWKKQE FSDPSLESQT
ADGTHGASQG VQQRMLSQQK RLLDQFTKHQ QGRLNSQRQK AQELDQLQAQ LETQLQEAEQ
TLISELSTLA RVPLPENKPF SNKRGLPEKP VRTKRKKPPP REREDLGTPN DDHLALADHT
TGPLSTTYSA SPPIRVHSGG RLDQQDSEAG DGESTSKILQ KGSNL
