CHODL_MOUSE
ID CHODL_MOUSE Reviewed; 273 AA.
AC Q9CXM0; Q3US20; Q8BVU2; Q8VI31;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Chondrolectin;
DE AltName: Full=Transmembrane protein MT75;
DE Flags: Precursor;
GN Name=Chodl;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J;
RX PubMed=12711387; DOI=10.1016/s0378-1119(03)00425-6;
RA Weng L., Huebner R., Claessens A., Smits P., Wauters J., Tylzanowski P.,
RA Van Marck E., Merregaert J.;
RT "Isolation and characterization of chondrolectin (Chodl), a novel C-type
RT lectin predominantly expressed in muscle cells.";
RL Gene 308:21-29(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic head, and Head;
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 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP INTERACTION WITH RABGGTB.
RX PubMed=18161010; DOI=10.2478/s11658-007-0052-8;
RA Claessens A., Weyn C., Merregaert J.;
RT "The cytoplasmic domain of chondrolectin interacts with the beta-subunit of
RT Rab geranylgeranyl transferase.";
RL Cell. Mol. Biol. Lett. 13:250-259(2008).
RN [6]
RP TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RX PubMed=20019802; DOI=10.1371/journal.pgen.1000773;
RA Baeumer D., Lee S., Nicholson G., Davies J.L., Parkinson N.J., Murray L.M.,
RA Gillingwater T.H., Ansorge O., Davies K.E., Talbot K.;
RT "Alternative splicing events are a late feature of pathology in a mouse
RT model of spinal muscular atrophy.";
RL PLoS Genet. 5:E1000773-E1000773(2009).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20437528; DOI=10.1002/cne.22332;
RA Enjin A., Rabe N., Nakanishi S.T., Vallstedt A., Gezelius H., Memic F.,
RA Lind M., Hjalt T., Tourtellotte W.G., Bruder C., Eichele G., Whelan P.J.,
RA Kullander K.;
RT "Identification of novel spinal cholinergic genetic subtypes disclose Chodl
RT and Pitx2 as markers for fast motor neurons and partition cells.";
RL J. Comp. Neurol. 518:2284-2304(2010).
RN [8]
RP FUNCTION, AND POSSIBLE INVOLVEMENT IN SMA.
RX PubMed=24067532; DOI=10.1093/hmg/ddt477;
RA Sleigh J.N., Barreiro-Iglesias A., Oliver P.L., Biba A., Becker T.,
RA Davies K.E., Becker C.G., Talbot K.;
RT "Chondrolectin affects cell survival and neuronal outgrowth in in vitro and
RT in vivo models of spinal muscular atrophy.";
RL Hum. Mol. Genet. 23:855-869(2014).
CC -!- FUNCTION: May play a role in the development of the nervous system such
CC as in neurite outgrowth and elongation (PubMed:24067532). May be
CC involved in motor axon growth and guidance (By similarity).
CC {ECO:0000250|UniProtKB:Q568T5, ECO:0000305|PubMed:24067532}.
CC -!- SUBUNIT: Interacts with RABGGTB (PubMed:18161010).
CC -!- INTERACTION:
CC Q9CXM0; P53612: Rabggtb; NbExp=2; IntAct=EBI-13948582, EBI-9104297;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.
CC {ECO:0000305|PubMed:20019802};
CC Name=1; Synonyms=Chodl-001;
CC IsoId=Q9CXM0-1; Sequence=Displayed;
CC Name=2; Synonyms=Chodl-002;
CC IsoId=Q9CXM0-2; Sequence=VSP_058918;
CC -!- TISSUE SPECIFICITY: In adult mice preferentially expressed in skeletal
CC muscle, testis, brain, and lung. Expressed in striated muscle (at
CC protein level). Expressed in spinal chord. Detected in spinal chord
CC fast motor neurons (at protein level). {ECO:0000269|PubMed:12711387,
CC ECO:0000269|PubMed:20019802, ECO:0000269|PubMed:20437528}.
CC -!- DEVELOPMENTAL STAGE: During gestation (7dpc to 15 dpc) its expression
CC is up-regulated. In 15 dpc embryo is expressed in muscle cells of
CC heterogeneous origin, including those from tongue, trunk, and tail. In
CC newborn mice localized to limb striated muscle cells. Expressed in
CC myoblasts undergoing myogenic differentiation during proliferation and
CC differentiation phases (PubMed:12711387). Expressed in spinal chord
CC motor neurons at 10.5 dpc. Detected in the plexus region of the
CC developing limb bud at 10.5 dpc and 11.5 dpc (PubMed:20437528).
CC {ECO:0000269|PubMed:12711387, ECO:0000269|PubMed:20437528}.
CC -!- MISCELLANEOUS: Isoform 1 but not isoform 2 expression is down-regulated
CC at postnatal day (P) 7 in spinal muscular atrophy (SMA) model motor
CC neurons before onset of disease. {ECO:0000269|PubMed:24067532}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Chondrolectin;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_335";
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DR EMBL; AF311699; AAL50354.1; -; mRNA.
DR EMBL; AK014255; BAB29226.1; -; mRNA.
DR EMBL; AK076523; BAC36378.1; -; mRNA.
DR EMBL; AK140910; BAE24517.1; -; mRNA.
DR EMBL; AC114925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117071; AAI17072.1; -; mRNA.
DR EMBL; BC117073; AAI17074.1; -; mRNA.
DR CCDS; CCDS28279.1; -. [Q9CXM0-1]
DR RefSeq; NP_624360.2; NM_139134.3. [Q9CXM0-1]
DR RefSeq; XP_006523093.1; XM_006523030.3. [Q9CXM0-2]
DR AlphaFoldDB; Q9CXM0; -.
DR SMR; Q9CXM0; -.
DR IntAct; Q9CXM0; 7.
DR STRING; 10090.ENSMUSP00000023568; -.
DR GlyGen; Q9CXM0; 1 site.
DR PhosphoSitePlus; Q9CXM0; -.
DR PaxDb; Q9CXM0; -.
DR PRIDE; Q9CXM0; -.
DR ProteomicsDB; 283831; -. [Q9CXM0-1]
DR ProteomicsDB; 283832; -. [Q9CXM0-2]
DR Antibodypedia; 2518; 135 antibodies from 24 providers.
DR DNASU; 246048; -.
DR Ensembl; ENSMUST00000023568; ENSMUSP00000023568; ENSMUSG00000022860. [Q9CXM0-1]
DR Ensembl; ENSMUST00000069148; ENSMUSP00000063961; ENSMUSG00000022860. [Q9CXM0-2]
DR GeneID; 246048; -.
DR KEGG; mmu:246048; -.
DR UCSC; uc007zsw.1; mouse. [Q9CXM0-1]
DR CTD; 140578; -.
DR MGI; MGI:2179069; Chodl.
DR VEuPathDB; HostDB:ENSMUSG00000022860; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00390000001844; -.
DR InParanoid; Q9CXM0; -.
DR OMA; VASATCC; -.
DR OrthoDB; 1005951at2759; -.
DR TreeFam; TF330715; -.
DR BioGRID-ORCS; 246048; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Chodl; mouse.
DR PRO; PR:Q9CXM0; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9CXM0; protein.
DR Bgee; ENSMUSG00000022860; Expressed in facial nucleus and 172 other tissues.
DR ExpressionAtlas; Q9CXM0; baseline and differential.
DR Genevisible; Q9CXM0; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC-UCL.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:0010975; P:regulation of neuron projection development; IGI:MGI.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Lectin; Membrane;
KW Neurogenesis; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..273
FT /note="Chondrolectin"
FT /id="PRO_0000017416"
FT TOPO_DOM 22..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..179
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 247..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 61..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 144..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 246..273
FT /note="SKGRSKTSPNQSTLWISKSTRKESGMEV -> RKARRHFIKDSTPLSSECLA
FT ESLNSNLVHMAGSLIPYHFQNNSPSLN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:20019802"
FT /id="VSP_058918"
FT CONFLICT 24
FT /note="V -> W (in Ref. 2; BAB29226)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="K -> T (in Ref. 1; AAL50354)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 273 AA; 30331 MW; F3EAE2B059D4EA28 CRC64;
MIRIASLLLG AALLCAQGAF ARRVVSGQKV CFADVKHPCY KMAYFHELSS RVSFQEARLA
CESEGGVLLS LENEAEQKLI ESMLQNLTKP GTGISDGDFW IGLLRSGDGQ TSGACPDLYQ
WSDGSSSQFR NWYTDEPSCG SEKCVVMYHQ PTANPGLGGP YLYQWNDDRC NMKHNYICKY
EPEIHPTEPA EKPYLTNQPE ETHENVVVTE AGIIPNLIYV IIPTIPLLLL ILVALGTCCF
QMLHKSKGRS KTSPNQSTLW ISKSTRKESG MEV
