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Database: UniProt
Entry: LBN_MOUSE
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Original site: 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   24-JAN-2024, entry version 127.
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   GlyCosmos; Q8K1G2; 3 sites, No reported glycans.
DR   GlyGen; Q8K1G2; 3 sites.
DR   iPTMnet; Q8K1G2; -.
DR   PhosphoSitePlus; Q8K1G2; -.
DR   jPOST; Q8K1G2; -.
DR   MaxQB; Q8K1G2; -.
DR   PaxDb; 10090-ENSMUSP00000055130; -.
DR   ProteomicsDB; 290011; -.
DR   Pumba; Q8K1G2; -.
DR   Antibodypedia; 22606; 141 antibodies from 30 providers.
DR   DNASU; 68525; -.
DR   Ensembl; ENSMUST00000056365.9; ENSMUSP00000055130.9; ENSMUSG00000050248.12.
DR   GeneID; 68525; -.
DR   KEGG; mmu:68525; -.
DR   UCSC; uc008xfr.2; mouse.
DR   AGR; MGI:1915775; -.
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; IFFAQIK; -.
DR   OrthoDB; 4261679at2759; -.
DR   PhylomeDB; Q8K1G2; -.
DR   TreeFam; TF331379; -.
DR   Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR   BioGRID-ORCS; 68525; 4 hits in 78 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 169 other cell types or 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: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/EVC.
DR   PANTHER; PTHR16795:SF14; LIMBIN; 1.
DR   PANTHER; PTHR16795; LIMBIN/ELLIS-VAN CREVELD PROTEIN; 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
//
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