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 27-MAR-2024, entry version 216. 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 38. 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; 9606-ENSP00000327368; -. DR PeptideAtlas; Q03692; -. DR ProteomicsDB; 58218; -. DR Antibodypedia; 32484; 170 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 AGR; HGNC:2185; -. DR CTD; 1300; -. DR DisGeNET; 1300; -. DR GeneCards; COL10A1; -. DR GeneReviews; COL10A1; -. DR HGNC; HGNC:2185; COL10A1. DR HPA; ENSG00000123500; Tissue enhanced (gallbladder, ovary). 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; YTYDEYS; -. DR OrthoDB; 5361230at2759; -. 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; 8 hits in 1134 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 cell types or tissues. DR ExpressionAtlas; Q03692; baseline and differential. 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; EXP:ComplexPortal. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; 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 PANTHER; PTHR15427:SF33; EMI DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR15427; EMILIN ELASTIN MICROFIBRIL INTERFACE-LOCATED PROTEIN ELASTIN MICROFIBRIL INTERFACER; 1. DR Pfam; PF00386; C1q; 1. DR Pfam; PF01391; Collagen; 2. DR PRINTS; PR00007; COMPLEMNTC1Q. DR SMART; SM00110; C1Q; 1. DR SUPFAM; SSF49842; TNF-like; 1. DR PROSITE; PS50871; C1Q; 1. DR Genevisible; Q03692; HS. 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 //