CHADL_HUMAN
ID CHADL_HUMAN Reviewed; 762 AA.
AC Q6NUI6; Q05CY2; Q4G0S0; Q5JY13; Q86XY1; Q96E60;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Chondroadherin-like protein;
DE Flags: Precursor;
GN Name=CHADL; Synonyms=SLRR4B;
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 GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [2]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [4]
RP FUNCTION, INTERACTION WITH COLLAGEN AND COLLAGEN FIBRILS, AND SUBCELLULAR
RP LOCATION.
RX PubMed=25451920; DOI=10.1074/jbc.m114.593541;
RA Tillgren V., Ho J.C., Oennerfjord P., Kalamajski S.;
RT "The novel small leucine-rich protein chondroadherin-like (CHADL) is
RT expressed in cartilage and modulates chondrocyte differentiation.";
RL J. Biol. Chem. 290:918-925(2015).
CC -!- FUNCTION: Potential negative modulator of chondrocyte differentiation.
CC Inhibits collagen fibrillogenesis in vitro. May influence chondrocyte's
CC differentiation by acting on its cellular collagenous microenvironment.
CC {ECO:0000269|PubMed:25451920}.
CC -!- SUBUNIT: Associates with collagen and binds to collagen fibrils.
CC {ECO:0000269|PubMed:25451920}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25451920}. Secreted,
CC extracellular space, extracellular matrix
CC {ECO:0000250|UniProtKB:E9Q7T7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NUI6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NUI6-2; Sequence=VSP_027735;
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class IV subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH19839.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH68590.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL035681; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60419.1; -; Genomic_DNA.
DR EMBL; BC012882; AAH12882.1; -; mRNA.
DR EMBL; BC019839; AAH19839.1; ALT_FRAME; mRNA.
DR EMBL; BC040188; AAH40188.1; -; mRNA.
DR EMBL; BC048421; AAH48421.1; -; mRNA.
DR EMBL; BC068590; AAH68590.1; ALT_INIT; mRNA.
DR CCDS; CCDS46715.1; -. [Q6NUI6-1]
DR RefSeq; NP_612490.1; NM_138481.1. [Q6NUI6-1]
DR AlphaFoldDB; Q6NUI6; -.
DR SMR; Q6NUI6; -.
DR BioGRID; 127285; 1.
DR STRING; 9606.ENSP00000216241; -.
DR GlyGen; Q6NUI6; 2 sites.
DR iPTMnet; Q6NUI6; -.
DR PhosphoSitePlus; Q6NUI6; -.
DR BioMuta; CHADL; -.
DR DMDM; 158563972; -.
DR MassIVE; Q6NUI6; -.
DR PaxDb; Q6NUI6; -.
DR PeptideAtlas; Q6NUI6; -.
DR PRIDE; Q6NUI6; -.
DR ProteomicsDB; 66680; -. [Q6NUI6-1]
DR ProteomicsDB; 66681; -. [Q6NUI6-2]
DR Antibodypedia; 332; 80 antibodies from 18 providers.
DR DNASU; 150356; -.
DR Ensembl; ENST00000216241.14; ENSP00000216241.9; ENSG00000100399.16. [Q6NUI6-1]
DR GeneID; 150356; -.
DR KEGG; hsa:150356; -.
DR MANE-Select; ENST00000216241.14; ENSP00000216241.9; NM_138481.2; NP_612490.1.
DR UCSC; uc003azq.5; human. [Q6NUI6-1]
DR CTD; 150356; -.
DR DisGeNET; 150356; -.
DR GeneCards; CHADL; -.
DR HGNC; HGNC:25165; CHADL.
DR HPA; ENSG00000100399; Tissue enriched (brain).
DR MIM; 616236; gene.
DR neXtProt; NX_Q6NUI6; -.
DR OpenTargets; ENSG00000100399; -.
DR PharmGKB; PA162382224; -.
DR VEuPathDB; HostDB:ENSG00000100399; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000154464; -.
DR HOGENOM; CLU_022061_0_0_1; -.
DR InParanoid; Q6NUI6; -.
DR OMA; EAQHATC; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q6NUI6; -.
DR TreeFam; TF337463; -.
DR PathwayCommons; Q6NUI6; -.
DR BioGRID-ORCS; 150356; 10 hits in 1066 CRISPR screens.
DR ChiTaRS; CHADL; human.
DR GenomeRNAi; 150356; -.
DR Pharos; Q6NUI6; Tbio.
DR PRO; PR:Q6NUI6; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q6NUI6; protein.
DR Bgee; ENSG00000100399; Expressed in C1 segment of cervical spinal cord and 111 other tissues.
DR ExpressionAtlas; Q6NUI6; baseline and differential.
DR Genevisible; Q6NUI6; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005518; F:collagen binding; IDA:UniProtKB.
DR GO; GO:0098633; F:collagen fibril binding; IDA:UniProtKB.
DR GO; GO:0030021; F:extracellular matrix structural constituent conferring compression resistance; ISS:BHF-UCL.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:1904027; P:negative regulation of collagen fibril organization; IDA:UniProtKB.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF13855; LRR_8; 5.
DR SMART; SM00369; LRR_TYP; 19.
DR SMART; SM00082; LRRCT; 2.
DR SMART; SM00013; LRRNT; 2.
DR PROSITE; PS51450; LRR; 18.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Leucine-rich repeat; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..762
FT /note="Chondroadherin-like protein"
FT /id="PRO_0000299548"
FT DOMAIN 31..62
FT /note="LRRNT 1"
FT REPEAT 87..108
FT /note="LRR 1"
FT REPEAT 111..132
FT /note="LRR 2"
FT REPEAT 135..156
FT /note="LRR 3"
FT REPEAT 159..180
FT /note="LRR 4"
FT REPEAT 183..204
FT /note="LRR 5"
FT REPEAT 207..228
FT /note="LRR 6"
FT REPEAT 231..252
FT /note="LRR 7"
FT REPEAT 255..276
FT /note="LRR 8"
FT REPEAT 279..300
FT /note="LRR 9"
FT DOMAIN 310..359
FT /note="LRRCT 1"
FT DOMAIN 387..425
FT /note="LRRNT 2"
FT REPEAT 426..447
FT /note="LRR 10"
FT REPEAT 450..471
FT /note="LRR 11"
FT REPEAT 474..495
FT /note="LRR 12"
FT REPEAT 498..519
FT /note="LRR 13"
FT REPEAT 522..543
FT /note="LRR 14"
FT REPEAT 546..566
FT /note="LRR 15"
FT REPEAT 570..591
FT /note="LRR 16"
FT REPEAT 594..615
FT /note="LRR 17"
FT REPEAT 619..640
FT /note="LRR 18"
FT REPEAT 644..665
FT /note="LRR 19"
FT DOMAIN 675..724
FT /note="LRRCT 2"
FT REGION 364..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 396..411
FT /evidence="ECO:0000250"
FT DISULFID 679..722
FT /evidence="ECO:0000250"
FT DISULFID 681..701
FT /evidence="ECO:0000250"
FT VAR_SEQ 662..737
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027735"
FT VARIANT 710
FT /note="Q -> R (in dbSNP:rs9619955)"
FT /id="VAR_059805"
FT VARIANT 721
FT /note="D -> N (in dbSNP:rs9619954)"
FT /id="VAR_061805"
FT CONFLICT 11
FT /note="P -> T (in Ref. 3; AAH40188)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="A -> T (in Ref. 3; AAH40188)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="E -> G (in Ref. 3; AAH40188)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="P -> R (in Ref. 3; AAH68590)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="L -> V (in Ref. 3; AAH40188)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="R -> S (in Ref. 3; AAH48421)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="Q -> H (in Ref. 3; AAH68590)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 762 AA; 82388 MW; BE01DF94D3408A70 CRC64;
MEGPRSSTHV PLVLPLLVLL LLAPARQAAA QRCPQACICD NSRRHVACRY QNLTEVPDAI
PELTQRLDLQ GNLLKVIPAA AFQGVPHLTH LDLRHCEVEL VAEGAFRGLG RLLLLNLASN
HLRELPQEAL DGLGSLRRLE LEGNALEELR PGTFGALGAL ATLNLAHNAL VYLPAMAFQG
LLRVRWLRLS HNALSVLAPE ALAGLPALRR LSLHHNELQA LPGPVLSQAR GLARLELGHN
PLTYAGEEDG LALPGLRELL LDGGALQALG PRAFAHCPRL HTLDLRGNQL DTLPPLQGPG
QLRRLRLQGN PLWCGCQARP LLEWLARARV RSDGACQGPR RLRGEALDAL RPWDLRCPGD
AAQEEEELEE RAVAGPRAPP RGPPRGPGEE RAVAPCPRAC VCVPESRHSS CEGCGLQAVP
RGFPSDTQLL DLRRNHFPSV PRAAFPGLGH LVSLHLQHCG IAELEAGALA GLGRLIYLYL
SDNQLAGLSA AALEGAPRLG YLYLERNRFL QVPGAALRAL PSLFSLHLQD NAVDRLAPGD
LGRTRALRWV YLSGNRITEV SLGALGPARE LEKLHLDRNQ LREVPTGALE GLPALLELQL
SGNPLRALRD GAFQPVGRSL QHLFLNSSGL EQICPGAFSG LGPGLQSLHL QKNQLRALPA
LPSLSQLELI DLSSNPFHCD CQLLPLHRWL TGLNLRVGAT CATPPNARGQ RVKAAAAVFE
DCPGWAARKA KRTPASRPSA RRTPIKGRQC GADKVGKEKG RL
