COAA1_HUMAN
ID COAA1_HUMAN Reviewed; 680 AA.
AC Q03692; A1L4P2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Collagen alpha-1(X) chain;
DE Flags: Precursor;
GN Name=COL10A1;
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 [GENOMIC DNA], AND VARIANT THR-27.
RX PubMed=1764025; DOI=10.1042/bj2800617;
RA Thomas J.T., Cresswell C.J., Rash B., Nicolai H., Jones T., Solomon E.,
RA Grant M.E., Boot-Handford R.P.;
RT "The human collagen X gene. Complete primary translated sequence and
RT chromosomal localization.";
RL Biochem. J. 280:617-623(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1397333; DOI=10.1016/0014-5793(92)81126-7;
RA Reichenberger E., Beier F., LuValle P., Olsen B.R., von der Mark K.,
RA Bertling W.M.;
RT "Genomic organization and full-length cDNA sequence of human collagen X.";
RL FEBS Lett. 311:305-310(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Beier F., Lammi M.B., von der Mark K.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-680.
RX PubMed=1587271; DOI=10.1111/j.1432-1033.1992.tb16919.x;
RA Apte S.S., Seldin M.F., Hayashi M., Olsen B.R.;
RT "Cloning of the human and mouse type X collagen genes and mapping of the
RT mouse type X collagen gene to chromosome 10.";
RL Eur. J. Biochem. 206:217-224(1992).
RN [8]
RP NUCLEOTIDE SEQUENCE OF 561-666.
RX PubMed=2037056; DOI=10.1016/0014-5793(91)80521-4;
RA Apte S., Mattei M.-G., Olsen B.R.;
RT "Cloning of human alpha 1(X) collagen DNA and localization of the COL10A1
RT gene to the q21-q22 region of human chromosome 6.";
RL FEBS Lett. 282:393-396(1991).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 547-655.
RX PubMed=1743401; DOI=10.1016/0012-1606(91)90274-7;
RA Reichenberger E., Aigner T., von der Mark K., Stoeb H., Bertling W.;
RT "In situ hybridization studies on the expression of type X collagen in
RT fetal human cartilage.";
RL Dev. Biol. 148:562-572(1991).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 521-680 IN COMPLEX WITH CALCIUM,
RP SUBUNIT, AND CALCIUM-BINDING.
RX PubMed=11839302; DOI=10.1016/s0969-2126(02)00697-4;
RA Bogin O., Kvansakul M., Rom E., Singer J., Yayon A., Hohenester E.;
RT "Insight into Schmid metaphyseal chondrodysplasia from the crystal
RT structure of the collagen X NC1 domain trimer.";
RL Structure 10:165-173(2002).
RN [11]
RP REVIEW ON VARIANTS.
RX PubMed=9101290;
RX DOI=10.1002/(sici)1098-1004(1997)9:4<300::aid-humu2>3.0.co;2-9;
RA Kuivaniemi H., Tromp G., Prockop D.J.;
RT "Mutations in fibrillar collagens (types I, II, III, and XI), fibril-
RT associated collagen (type IX), and network-forming collagen (type X) cause
RT a spectrum of diseases of bone, cartilage, and blood vessels.";
RL Hum. Mutat. 9:300-315(1997).
RN [12]
RP VARIANTS SMCD ASP-598 AND PRO-614.
RX PubMed=8304336;
RA Wallis G.A., Rash B., Sweetman W.A., Thomas J.T., Super M., Evans G.,
RA Grant M.E., Boot-Handford R.P.;
RT "Amino acid substitutions of conserved residues in the carboxyl-terminal
RT domain of the alpha 1(X) chain of type X collagen occur in two unrelated
RT families with metaphyseal chondrodysplasia type Schmid.";
RL Am. J. Hum. Genet. 54:169-178(1994).
RN [13]
RP VARIANT SMCD ARG-591.
RX PubMed=8004099; DOI=10.1093/hmg/3.2.303;
RA McIntosh I., Abbott M.H., Warman M.L., Olsen B.R., Francomano C.A.;
RT "Additional mutations of type X collagen confirm COL10A1 as the Schmid
RT metaphyseal chondrodysplasia locus.";
RL Hum. Mol. Genet. 3:303-307(1994).
RN [14]
RP VARIANT SMCD VAL-618.
RX PubMed=7876225; DOI=10.1074/jbc.270.9.4558;
RA Chan D., Cole W.G., Rogers J.G., Bateman J.F.;
RT "Type X collagen multimer assembly in vitro is prevented by a Gly618 to Val
RT mutation in the alpha 1(X) NC1 domain resulting in Schmid metaphyseal
RT chondrodysplasia.";
RL J. Biol. Chem. 270:4558-4562(1995).
RN [15]
RP VARIANTS SMCD ARG-545; GLU-595; HIS-597; LYS-617; ARG-644 AND GLY-648.
RX PubMed=7607655; DOI=10.1007/bf00214187;
RA Bonaventure J., Chaminade F., Maroteaux P.;
RT "Mutations in three subdomains of the carboxy-terminal region of collagen
RT type X account for most of the Schmid metaphyseal dysplasias.";
RL Hum. Genet. 96:58-64(1995).
RN [16]
RP VARIANT SMCD PRO-600.
RX PubMed=8782043; DOI=10.1136/jmg.33.6.450;
RA Wallis G.A., Rash B., Sykes B., Bonaventure J., Maroteaux P., Zabel B.,
RA Wynne-Davies R., Grant M.E., Boot-Handford R.P.;
RT "Mutations within the gene encoding the alpha 1 (X) chain of type X
RT collagen (COL10A1) cause metaphyseal chondrodysplasia type Schmid but not
RT several other forms of metaphyseal chondrodysplasia.";
RL J. Med. Genet. 33:450-457(1996).
RN [17]
RP VARIANTS SMCD GLU-18 AND ARG-18.
RX PubMed=9067753;
RX DOI=10.1002/(sici)1098-1004(1997)9:2<131::aid-humu5>3.0.co;2-c;
RA Ikegawa S., Nakamura K., Nagano A., Haga N., Nakamura Y.;
RT "Mutations in the N-terminal globular domain of the type X collagen gene
RT (COL10A1) in patients with schmid metaphyseal chondrodysplasia.";
RL Hum. Mutat. 9:131-135(1997).
RN [18]
RP VARIANT SPONDYLOMETAPHYSEAL DYSPLASIA JAPANESE TYPE GLU-595.
RX PubMed=9837818; DOI=10.1086/302158;
RA Ikegawa S., Nishimura G., Nagai T., Hasegawa T., Ohashi H., Nakamura Y.;
RT "Mutation of the type X collagen gene 'COL10A1' causes spondylometaphyseal
RT dysplasia.";
RL Am. J. Hum. Genet. 63:1659-1662(1998).
RN [19]
RP VARIANT SMCD CYS-597.
RX PubMed=9852679; DOI=10.1007/s100380050085;
RA Sawai H., Ida A., Nakata Y., Koyama K.;
RT "Novel missense mutation resulting in the substitution of tyrosine by
RT cysteine at codon 597 of the type X collagen gene associated with Schmid
RT metaphyseal chondrodysplasia.";
RL J. Hum. Genet. 43:259-261(1998).
RN [20]
RP VARIANTS SMCD ARG-18; GLU-18; ASP-582; ARG-591; ARG-595; GLU-595; HIS-597;
RP CYS-597; ASP-598; PRO-600; PRO-614; LYS-617; VAL-618; ARG-644; GLY-648;
RP ARG-651; PRO-653 AND PRO-671, AND VARIANTS THR-27; HIS-198; ARG-545 AND
RP MET-603.
RX PubMed=15880705; DOI=10.1002/humu.20183;
RA Bateman J.F., Wilson R., Freddi S., Lamande S.R., Savarirayan R.;
RT "Mutations of COL10A1 in Schmid metaphyseal chondrodysplasia.";
RL Hum. Mutat. 25:525-534(2005).
CC -!- FUNCTION: Type X collagen is a product of hypertrophic chondrocytes and
CC has been localized to presumptive mineralization zones of hyaline
CC cartilage.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:11839302}.
CC -!- INTERACTION:
CC Q03692; Q8N9N5: BANP; NbExp=3; IntAct=EBI-2528309, EBI-744695;
CC Q03692; Q8N9N5-2: BANP; NbExp=6; IntAct=EBI-2528309, EBI-11524452;
CC Q03692; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-2528309, EBI-7062247;
CC Q03692; Q14696: MESD; NbExp=3; IntAct=EBI-2528309, EBI-6165891;
CC Q03692; Q16656-4: NRF1; NbExp=3; IntAct=EBI-2528309, EBI-11742836;
CC Q03692; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-2528309, EBI-744081;
CC Q03692; Q9UMX0: UBQLN1; NbExp=6; IntAct=EBI-2528309, EBI-741480;
CC Q03692; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-2528309, EBI-10173939;
CC Q03692; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-2528309, EBI-947187;
CC Q03692; P62760: VSNL1; NbExp=3; IntAct=EBI-2528309, EBI-740943;
CC Q03692; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-2528309, EBI-11741890;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) are hydroxylated in some or all of the chains.
CC -!- DISEASE: Schmid type metaphyseal chondrodysplasia (SMCD) [MIM:156500]:
CC Dominantly inherited disorder of the osseous skeleton. The cardinal
CC features of the phenotype are mild short stature, coxa vara and a
CC waddling gait. Radiography usually shows sclerosis of the ribs, flaring
CC of the metaphyses, and a wide irregular growth plate, especially of the
CC knees. A variant form of SMCD is spondylometaphyseal dysplasia Japanese
CC type. It is characterized by spinal involvement comprising mild
CC platyspondyly, vertebral body abnormalities, and end-plate
CC irregularity. {ECO:0000269|PubMed:15880705, ECO:0000269|PubMed:7607655,
CC ECO:0000269|PubMed:7876225, ECO:0000269|PubMed:8004099,
CC ECO:0000269|PubMed:8304336, ECO:0000269|PubMed:8782043,
CC ECO:0000269|PubMed:9067753, ECO:0000269|PubMed:9852679}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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DR EMBL; X60382; CAA42933.1; -; Genomic_DNA.
DR EMBL; X72579; CAA51170.1; -; Genomic_DNA.
DR EMBL; X72580; CAA51170.1; JOINED; Genomic_DNA.
DR EMBL; X98568; CAA67178.1; -; Genomic_DNA.
DR EMBL; AL121963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48240.1; -; Genomic_DNA.
DR EMBL; BC130621; AAI30622.1; -; mRNA.
DR EMBL; BC130623; AAI30624.1; -; mRNA.
DR EMBL; X65120; CAA46236.1; -; Genomic_DNA.
DR EMBL; X58879; CAA41686.1; -; Genomic_DNA.
DR EMBL; M74050; AAA61221.1; -; Genomic_DNA.
DR EMBL; S68531; AAC60615.1; -; mRNA.
DR CCDS; CCDS5105.1; -.
DR PIR; S26396; CGHU1D.
DR RefSeq; NP_000484.2; NM_000493.3.
DR RefSeq; XP_006715396.1; XM_006715333.3.
DR RefSeq; XP_011533734.1; XM_011535432.2.
DR RefSeq; XP_011533735.1; XM_011535433.2.
DR RefSeq; XP_016865737.1; XM_017010248.1.
DR RefSeq; XP_016865738.1; XM_017010249.1.
DR PDB; 1GR3; X-ray; 2.00 A; A=521-680.
DR PDBsum; 1GR3; -.
DR AlphaFoldDB; Q03692; -.
DR SMR; Q03692; -.
DR BioGRID; 107697; 36.
DR ComplexPortal; CPX-1749; Collagen type X trimer.
DR IntAct; Q03692; 16.
DR MINT; Q03692; -.
DR STRING; 9606.ENSP00000327368; -.
DR PhosphoSitePlus; Q03692; -.
DR BioMuta; COL10A1; -.
DR DMDM; 2506306; -.
DR jPOST; Q03692; -.
DR MassIVE; Q03692; -.
DR PaxDb; Q03692; -.
DR PeptideAtlas; Q03692; -.
DR PRIDE; Q03692; -.
DR ProteomicsDB; 58218; -.
DR Antibodypedia; 32484; 151 antibodies from 23 providers.
DR DNASU; 1300; -.
DR Ensembl; ENST00000243222.8; ENSP00000243222.4; ENSG00000123500.10.
DR Ensembl; ENST00000327673.4; ENSP00000327368.4; ENSG00000123500.10.
DR Ensembl; ENST00000651968.1; ENSP00000498802.1; ENSG00000123500.10.
DR GeneID; 1300; -.
DR KEGG; hsa:1300; -.
DR MANE-Select; ENST00000651968.1; ENSP00000498802.1; NM_000493.4; NP_000484.2.
DR UCSC; uc003pwm.4; human.
DR CTD; 1300; -.
DR DisGeNET; 1300; -.
DR GeneCards; COL10A1; -.
DR GeneReviews; COL10A1; -.
DR HGNC; HGNC:2185; COL10A1.
DR HPA; ENSG00000123500; Group enriched (brain, choroid plexus, gallbladder).
DR MalaCards; COL10A1; -.
DR MIM; 120110; gene.
DR MIM; 156500; phenotype.
DR neXtProt; NX_Q03692; -.
DR OpenTargets; ENSG00000123500; -.
DR Orphanet; 174; Metaphyseal chondrodysplasia, Schmid type.
DR PharmGKB; PA26701; -.
DR VEuPathDB; HostDB:ENSG00000123500; -.
DR eggNOG; ENOG502QS5V; Eukaryota.
DR GeneTree; ENSGT00940000154317; -.
DR HOGENOM; CLU_001074_21_0_1; -.
DR InParanoid; Q03692; -.
DR OMA; DEYIKGY; -.
DR OrthoDB; 1167208at2759; -.
DR PhylomeDB; Q03692; -.
DR TreeFam; TF334029; -.
DR PathwayCommons; Q03692; -.
DR Reactome; R-HSA-1442490; Collagen degradation.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-HSA-8948216; Collagen chain trimerization.
DR SignaLink; Q03692; -.
DR SIGNOR; Q03692; -.
DR BioGRID-ORCS; 1300; 7 hits in 1056 CRISPR screens.
DR ChiTaRS; COL10A1; human.
DR EvolutionaryTrace; Q03692; -.
DR GeneWiki; Collagen,_type_X,_alpha_1; -.
DR GenomeRNAi; 1300; -.
DR Pharos; Q03692; Tbio.
DR PRO; PR:Q03692; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q03692; protein.
DR Bgee; ENSG00000123500; Expressed in tibia and 123 other tissues.
DR ExpressionAtlas; Q03692; baseline and differential.
DR Genevisible; Q03692; HS.
DR GO; GO:0005581; C:collagen trimer; TAS:ProtInc.
DR GO; GO:0005599; C:collagen type X trimer; IPI:ComplexPortal.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR Pfam; PF00386; C1q; 1.
DR Pfam; PF01391; Collagen; 3.
DR PRINTS; PR00007; COMPLEMNTC1Q.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50871; C1Q; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Collagen; Disease variant; Extracellular matrix;
KW Hydroxylation; Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..680
FT /note="Collagen alpha-1(X) chain"
FT /id="PRO_0000005770"
FT DOMAIN 547..680
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 19..56
FT /note="Nonhelical region (NC2)"
FT REGION 55..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..519
FT /note="Triple-helical region"
FT REGION 520..680
FT /note="Nonhelical region (NC1)"
FT COMPBIAS 63..83
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..107
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..151
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..424
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..476
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..519
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 626
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11839302,
FT ECO:0007744|PDB:1GR3"
FT BINDING 627
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11839302,
FT ECO:0007744|PDB:1GR3"
FT BINDING 633
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11839302,
FT ECO:0007744|PDB:1GR3"
FT BINDING 634
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11839302,
FT ECO:0007744|PDB:1GR3"
FT BINDING 634
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000269|PubMed:11839302,
FT ECO:0007744|PDB:1GR3"
FT VARIANT 18
FT /note="G -> E (in SMCD; dbSNP:rs111033551)"
FT /evidence="ECO:0000269|PubMed:15880705,
FT ECO:0000269|PubMed:9067753"
FT /id="VAR_001838"
FT VARIANT 18
FT /note="G -> R (in SMCD; dbSNP:rs111033550)"
FT /evidence="ECO:0000269|PubMed:15880705,
FT ECO:0000269|PubMed:9067753"
FT /id="VAR_001839"
FT VARIANT 27
FT /note="M -> T (in dbSNP:rs1064583)"
FT /evidence="ECO:0000269|PubMed:15880705,
FT ECO:0000269|PubMed:1764025"
FT /id="VAR_023186"
FT VARIANT 98
FT /note="G -> R (in dbSNP:rs2243370)"
FT /id="VAR_048767"
FT VARIANT 198
FT /note="R -> H (in dbSNP:rs148785195)"
FT /evidence="ECO:0000269|PubMed:15880705"
FT /id="VAR_023187"
FT VARIANT 545
FT /note="G -> R (in dbSNP:rs2228547)"
FT /evidence="ECO:0000269|PubMed:15880705,
FT ECO:0000269|PubMed:7607655"
FT /id="VAR_001840"
FT VARIANT 582
FT /note="Y -> D (in SMCD)"
FT /evidence="ECO:0000269|PubMed:15880705"
FT /id="VAR_023188"
FT VARIANT 591
FT /note="C -> R (in SMCD; dbSNP:rs111033546)"
FT /evidence="ECO:0000269|PubMed:15880705,
FT ECO:0000269|PubMed:8004099"
FT /id="VAR_001841"
FT VARIANT 595
FT /note="G -> E (in SMCD and spondylometaphyseal dysplasia
FT Japanese type; dbSNP:rs111033553)"
FT /evidence="ECO:0000269|PubMed:15880705,
FT ECO:0000269|PubMed:7607655, ECO:0000269|PubMed:9837818"
FT /id="VAR_001842"
FT VARIANT 595
FT /note="G -> R (in SMCD)"
FT /evidence="ECO:0000269|PubMed:15880705"
FT /id="VAR_023189"
FT VARIANT 597
FT /note="Y -> C (in SMCD; dbSNP:rs111033554)"
FT /evidence="ECO:0000269|PubMed:15880705,
FT ECO:0000269|PubMed:9852679"
FT /id="VAR_008039"
FT VARIANT 597
FT /note="Y -> H (in SMCD)"
FT /evidence="ECO:0000269|PubMed:15880705,
FT ECO:0000269|PubMed:7607655"
FT /id="VAR_001843"
FT VARIANT 598
FT /note="Y -> D (in SMCD; dbSNP:rs111033544)"
FT /evidence="ECO:0000269|PubMed:15880705,
FT ECO:0000269|PubMed:8304336"
FT /id="VAR_001844"
FT VARIANT 600
FT /note="S -> P (in SMCD; dbSNP:rs111033555)"
FT /evidence="ECO:0000269|PubMed:15880705,
FT ECO:0000269|PubMed:8782043"
FT /id="VAR_001845"
FT VARIANT 603
FT /note="V -> M (in dbSNP:rs143769451)"
FT /evidence="ECO:0000269|PubMed:15880705"
FT /id="VAR_023190"
FT VARIANT 614
FT /note="L -> P (in SMCD; dbSNP:rs111033545)"
FT /evidence="ECO:0000269|PubMed:15880705,
FT ECO:0000269|PubMed:8304336"
FT /id="VAR_001846"
FT VARIANT 617
FT /note="N -> K (in SMCD)"
FT /evidence="ECO:0000269|PubMed:15880705,
FT ECO:0000269|PubMed:7607655"
FT /id="VAR_001847"
FT VARIANT 618
FT /note="G -> V (in SMCD)"
FT /evidence="ECO:0000269|PubMed:15880705,
FT ECO:0000269|PubMed:7876225"
FT /id="VAR_001848"
FT VARIANT 644
FT /note="L -> R (in SMCD)"
FT /evidence="ECO:0000269|PubMed:15880705,
FT ECO:0000269|PubMed:7607655"
FT /id="VAR_001849"
FT VARIANT 648
FT /note="D -> G (in SMCD)"
FT /evidence="ECO:0000269|PubMed:15880705,
FT ECO:0000269|PubMed:7607655"
FT /id="VAR_001850"
FT VARIANT 651
FT /note="W -> R (in SMCD; dbSNP:rs111033549)"
FT /evidence="ECO:0000269|PubMed:15880705"
FT /id="VAR_023191"
FT VARIANT 653
FT /note="Q -> P (in SMCD; dbSNP:rs1271742789)"
FT /evidence="ECO:0000269|PubMed:15880705"
FT /id="VAR_023192"
FT VARIANT 671
FT /note="S -> P (in SMCD; dbSNP:rs111033552)"
FT /evidence="ECO:0000269|PubMed:15880705"
FT /id="VAR_023193"
FT CONFLICT 500
FT /note="H -> P (in Ref. 1; CAA42933)"
FT /evidence="ECO:0000305"
FT STRAND 553..557
FT /evidence="ECO:0007829|PDB:1GR3"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:1GR3"
FT STRAND 573..576
FT /evidence="ECO:0007829|PDB:1GR3"
FT TURN 584..586
FT /evidence="ECO:0007829|PDB:1GR3"
FT STRAND 595..616
FT /evidence="ECO:0007829|PDB:1GR3"
FT STRAND 619..626
FT /evidence="ECO:0007829|PDB:1GR3"
FT STRAND 634..644
FT /evidence="ECO:0007829|PDB:1GR3"
FT STRAND 649..653
FT /evidence="ECO:0007829|PDB:1GR3"
FT STRAND 659..663
FT /evidence="ECO:0007829|PDB:1GR3"
FT STRAND 666..668
FT /evidence="ECO:0007829|PDB:1GR3"
FT STRAND 671..679
FT /evidence="ECO:0007829|PDB:1GR3"
SQ SEQUENCE 680 AA; 66158 MW; E2F98E53E7882459 CRC64;
MLPQIPFLLL VSLNLVHGVF YAERYQMPTG IKGPLPNTKT QFFIPYTIKS KGIAVRGEQG
TPGPPGPAGP RGHPGPSGPP GKPGYGSPGL QGEPGLPGPP GPSAVGKPGV PGLPGKPGER
GPYGPKGDVG PAGLPGPRGP PGPPGIPGPA GISVPGKPGQ QGPTGAPGPR GFPGEKGAPG
VPGMNGQKGE MGYGAPGRPG ERGLPGPQGP TGPSGPPGVG KRGENGVPGQ PGIKGDRGFP
GEMGPIGPPG PQGPPGERGP EGIGKPGAAG APGQPGIPGT KGLPGAPGIA GPPGPPGFGK
PGLPGLKGER GPAGLPGGPG AKGEQGPAGL PGKPGLTGPP GNMGPQGPKG IPGSHGLPGP
KGETGPAGPA GYPGAKGERG SPGSDGKPGY PGKPGLDGPK GNPGLPGPKG DPGVGGPPGL
PGPVGPAGAK GMPGHNGEAG PRGAPGIPGT RGPIGPPGIP GFPGSKGDPG SPGPPGPAGI
ATKGLNGPTG PPGPPGPRGH SGEPGLPGPP GPPGPPGQAV MPEGFIKAGQ RPSLSGTPLV
SANQGVTGMP VSAFTVILSK AYPAIGTPIP FDKILYNRQQ HYDPRTGIFT CQIPGIYYFS
YHVHVKGTHV WVGLYKNGTP VMYTYDEYTK GYLDQASGSA IIDLTENDQV WLQLPNAESN
GLYSSEYVHS SFSGFLVAPM
