LBN_MOUSE
ID LBN_MOUSE Reviewed; 1220 AA.
AC Q8K1G2; Q8BRF3;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Limbin;
DE Flags: Precursor;
GN Name=Evc2; Synonyms=Lbn;
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 TISSUE SPECIFICITY.
RC TISSUE=Limb bud;
RX PubMed=12136126; DOI=10.1073/pnas.152337899;
RA Takeda H., Takami M., Oguni T., Tsuji T., Yoneda K., Sato H., Ihara N.,
RA Itoh T., Kata S.R., Mishina Y., Womack J.E., Moritomo Y., Sugimoto Y.,
RA Kunieda T.;
RT "Positional cloning of the gene LIMBIN responsible for bovine
RT chondrodysplastic dwarfism.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10549-10554(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney, and Mammary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-744.
RC STRAIN=C57BL/6J;
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 [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND INTERACTION WITH EVC.
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 [6]
RP FUNCTION, IDENTIFICATION IN THE EVC COMPLEX, INTERACTION WITH EFCAB7; EVC
RP AND IQCE, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 1185-PHE--ARG-1188.
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:21356043, PubMed:24582806).
CC Plays a critical role in bone formation and skeletal development
CC (PubMed:21356043). May be involved in early embryonic morphogenesis
CC (PubMed:21356043). {ECO:0000269|PubMed:21356043,
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 EVC (PubMed:21356043,
CC PubMed:24582806). Interacts (via N-terminal end) with EFCAB7
CC (PubMed:24582806). Interacts (via N-terminal end) with IQCE
CC (PubMed:24582806). {ECO:0000269|PubMed:24582806}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21356043};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:21356043}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:21356043}. Cell projection, cilium
CC {ECO:0000269|PubMed:21356043}. Cell projection, cilium membrane
CC {ECO:0000269|PubMed:21356043, ECO:0000269|PubMed:24582806}. Nucleus
CC {ECO:0000269|PubMed:21356043}. 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 -!- TISSUE SPECIFICITY: Expressed in long and cranial bones, kidney and
CC heart. Strongly expressed in proliferating chondrocytes, osteoblasts
CC and osteoclasts. {ECO:0000269|PubMed:12136126}.
CC -!- DEVELOPMENTAL STAGE: Found in the embryo at day 7 dpc, 11 dpc, 15 dpc,
CC and 17 dpc. At the limb bud formation stage 11 dpc, it is expressed in
CC fore- and hindlimb buds, branchial arches, and facial primordia.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC32167.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB083066; BAC06589.1; -; mRNA.
DR EMBL; BC037473; AAH37473.1; -; mRNA.
DR EMBL; BC064473; AAH64473.1; -; mRNA.
DR EMBL; AK044977; BAC32167.1; ALT_INIT; mRNA.
DR CCDS; CCDS19248.1; -.
DR RefSeq; NP_666032.1; NM_145920.3.
DR AlphaFoldDB; Q8K1G2; -.
DR SMR; Q8K1G2; -.
DR STRING; 10090.ENSMUSP00000055130; -.
DR GlyGen; Q8K1G2; 3 sites.
DR iPTMnet; Q8K1G2; -.
DR PhosphoSitePlus; Q8K1G2; -.
DR jPOST; Q8K1G2; -.
DR MaxQB; Q8K1G2; -.
DR PaxDb; Q8K1G2; -.
DR PRIDE; Q8K1G2; -.
DR ProteomicsDB; 290011; -.
DR Antibodypedia; 22606; 134 antibodies from 30 providers.
DR DNASU; 68525; -.
DR Ensembl; ENSMUST00000056365; ENSMUSP00000055130; ENSMUSG00000050248.
DR GeneID; 68525; -.
DR KEGG; mmu:68525; -.
DR UCSC; uc008xfr.2; mouse.
DR CTD; 132884; -.
DR MGI; MGI:1915775; Evc2.
DR VEuPathDB; HostDB:ENSMUSG00000050248; -.
DR eggNOG; ENOG502QQ5U; Eukaryota.
DR GeneTree; ENSGT00940000154127; -.
DR HOGENOM; CLU_007621_0_0_1; -.
DR InParanoid; Q8K1G2; -.
DR OMA; QYLRQWR; -.
DR OrthoDB; 90381at2759; -.
DR PhylomeDB; Q8K1G2; -.
DR TreeFam; TF331379; -.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR BioGRID-ORCS; 68525; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Evc2; mouse.
DR PRO; PR:Q8K1G2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8K1G2; protein.
DR Bgee; ENSMUSG00000050248; Expressed in humerus cartilage element and 168 other tissues.
DR Genevisible; Q8K1G2; MM.
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:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0098797; C:plasma membrane protein complex; IDA:UniProtKB.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:UniProtKB.
DR InterPro; IPR022076; Limbin.
DR InterPro; IPR026501; Limbin/Ellis-van_Creveld.
DR PANTHER; PTHR16795; PTHR16795; 1.
DR Pfam; PF12297; EVC2_like; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cilium; Coiled coil; Cytoplasm;
KW Cytoskeleton; Glycoprotein; Membrane; Nucleus; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1220
FT /note="Limbin"
FT /id="PRO_0000084364"
FT TOPO_DOM 30..210
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..1220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 38..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 355..404
FT /evidence="ECO:0000255"
FT COILED 563..644
FT /evidence="ECO:0000255"
FT COILED 854..875
FT /evidence="ECO:0000255"
FT COILED 920..1005
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT MUTAGEN 1185..1188
FT /note="FVFR->AAAA: Inhibits interaction with EFCAB7."
FT /evidence="ECO:0000269|PubMed:24582806"
SQ SEQUENCE 1220 AA; 137639 MW; E67671714A866B1D CRC64;
MGATGPTGAG GRATWVLAGN ILAAALVLGS GPRALPPSFP ALGPGSPSRP GPAGPWASSQ
YSDISREARG PFENGVIFQK CSLVSGQSES QTMHVQLSVN NTRTPTSVNL SNLLVLDEIT
GLAVKESPGN NTQDGIQTFR KSFLQVGECY SVSYTASLDP TALGTGESLD LPARLIFQSP
SQNRTQLKAP FTITVEEKIM VLPNHGLHAA GFIAAFLISL LLTVAALFFL ARGRCLQGGM
LSRCRIQHPE NKLEPSPFTS ANGVSQDLSL NDQVVAILTS EEPGSMLQAL EELEIATLNQ
ADADLEACRN QISKDIIALL MKNLVSGGHL SPQTERKMAA AFKKQFLLLE NEIQEEYERK
MLALTAECDL EMRKKTENQY QREMVAMEEA EEVLKRVSER SAAECSSLLR TLHGLEQEDM
QRSLTLDQAE DFAQAHRQLA VFQRNELHSI VYTQIQSAVS KGELRPEVAK MMLQDYSKTQ
ESVEELMDFF QATKRYHLSK RFGHREYLVQ RLQAMETRVQ GLLNTAATQL TSLIHKHERA
GYLDEDQMET LLERAQTETF SIKQKLDNDL KQEKKRLHQR LITRRRRELL QKHKEQQKEQ
VSLGEASSTA EDAVQYLHQW RSVMAEHTAA LEELQERLDQ AALDDLRVLT VSLSEKATEE
LRRLQSTAMT QELLKRSAPW LFLQQILEEH SRESAARTTQ LEAEERERGQ ELVQGVRQRL
QQDALEAYTE EQAELRHWEH LVFMKLCCAA ISLSEEDLLR VRQEAQGCFS QLDRSLALPR
VRARVLQQQA QMAWREAEFR KLDQALAAPE LQSKARKLRS KGRGKADLLK KNLEDKIRLF
EERAPVELAD QVRGELLQER VQRLEAQEAH FAESLVALQF QKVARAAETL SVYTALLSIQ
DLLLGELSES ETLTKSACVQ ILESHRPELQ ELQELERKLE DQLVQQEEAE QQRVLESWQR
WAADGPGLSE PEEMDPERQV SAILRQALNK GQKLLEQHQQ RVREEWQNGA VLEDSLESIE
ADTMASLCSQ GLRLVSYLSR MTMVPGSTLL RLLSVVLPAA SQPQLLALLD AVSEKHSDHT
AENESSGEQA QAEQSKRRKH QVWWKVLDSR FRADLVSQGL ERMLWARQKK ERILKKIYVP
VQERVMFPGK GSWPHLSLEP IGELAPIPIT GADAMDILNT GEKIFVFRSP REPEISLRVP
PRRKKNFLNA KKANRALGLD
