ID   CO9A3_HUMAN             Reviewed;         684 AA.
AC   Q14050; Q13681; Q9H4G9; Q9UPE2;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   27-MAR-2024, entry version 203.
DE   RecName: Full=Collagen alpha-3(IX) chain;
DE   Flags: Precursor;
GN   Name=COL9A3;
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 [MRNA], AND VARIANT GLU-435.
RC   TISSUE=Cartilage;
RX   PubMed=8586434; DOI=10.1006/geno.1995.9870;
RA   Brewton R.G., Wood B.M., Ren Z.-X., Gong Y., Tiller G.E., Warman M.L.,
RA   Lee B., Horton W.A., Olsen B.R., Baker J.R., Mayne R.;
RT   "Molecular cloning of the alpha 3 chain of human type IX collagen: linkage
RT   of the gene COL9A3 to chromosome 20q13.3.";
RL   Genomics 30:329-336(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS 563-GLY--PRO-565 DEL AND
RP   564-PRO--GLY-566 DEL.
RX   PubMed=10428822; DOI=10.1074/jbc.274.32.22469;
RA   Paassilta P., Pihlajamaa T., Annunen S., Brewton R.G., Wood B.M.,
RA   Johnson C.C., Liu J., Gong Y., Warman M.L., Prockop D.J., Mayne R.,
RA   Ala-Kokko L.;
RT   "Complete sequence of the 23-kilobase human COL9A3 gene. Detection of Gly-
RT   X-Y triplet deletions that represent neutral variants.";
RL   J. Biol. Chem. 274:22469-22475(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 522-667.
RC   TISSUE=Cartilage;
RX   PubMed=9164858; DOI=10.1042/bj3240209;
RA   Peraelae M., Savontaus M., Metsaeranta M., Vuorio E.;
RT   "Developmental regulation of mRNA species for types II, IX and XI collagens
RT   during mouse embryogenesis.";
RL   Biochem. J. 324:209-216(1997).
RN   [6]
RP   INVOLVEMENT IN EDM3.
RX   PubMed=10090888; DOI=10.1086/302328;
RA   Paassilta P., Lohiniva J., Annunen S., Bonaventure J., Le Merrer M.,
RA   Pai L., Ala-Kokko L.;
RT   "COL9A3: A third locus for multiple epiphyseal dysplasia.";
RL   Am. J. Hum. Genet. 64:1036-1044(1999).
RN   [7]
RP   ERRATUM OF PUBMED:10090888.
RA   Paassilta P., Lohiniva J., Annunen S., Bonaventure J., Le Merrer M.,
RA   Pai L., Ala-Kokko L.;
RL   Am. J. Hum. Genet. 65:1214-1214(1999).
RN   [8]
RP   INVOLVEMENT IN SUSCEPTIBILITY TO IDD.
RX   PubMed=11308397; DOI=10.1001/jama.285.14.1843;
RA   Paassilta P., Lohiniva J., Goring H.H., Perala M., Raina S.S.,
RA   Karppinen J., Hakala M., Palm T., Kroger H., Kaitila I., Vanharanta H.,
RA   Ott J., Ala-Kokko L.;
RT   "Identification of a novel common genetic risk factor for lumbar disk
RT   disease.";
RL   JAMA 285:1843-1849(2001).
RN   [9]
RP   INVOLVEMENT IN STL6.
RX   PubMed=24273071; DOI=10.1002/ajmg.a.36165;
RA   Faletra F., D'Adamo A.P., Bruno I., Athanasakis E., Biskup S., Esposito L.,
RA   Gasparini P.;
RT   "Autosomal recessive Stickler syndrome due to a loss of function mutation
RT   in the COL9A3 gene.";
RL   Am. J. Med. Genet. A 164A:42-47(2014).
RN   [10]
RP   INVOLVEMENT IN STL6.
RX   PubMed=30450842; DOI=10.1002/ajmg.a.40647;
RG   University of Washington Center for Mendelian Genomics;
RA   Hanson-Kahn A., Li B., Cohn D.H., Nickerson D.A., Bamshad M.J., Hudgins L.;
RT   "Autosomal recessive Stickler syndrome resulting from a COL9A3 mutation.";
RL   Am. J. Med. Genet. A 176:2887-2891(2018).
RN   [11]
RP   VARIANTS GLN-103; TRP-103; LEU-296; GLN-402 AND GLU-435.
RX   PubMed=11565064; DOI=10.1086/324023;
RA   Czarny-Ratajczak M., Lohiniva J., Rogala P., Kozlowski K., Peraelae M.,
RA   Carter L., Spector T.D., Kolodziej L., Seppaenen U., Glazar R.,
RA   Krolewski J., Latos-Bielenska A., Ala-Kokko L.;
RT   "A mutation in COL9A1 causes multiple epiphyseal dysplasia: further
RT   evidence for locus heterogeneity.";
RL   Am. J. Hum. Genet. 69:969-980(2001).
RN   [12]
RP   VARIANT EDM3 ASP-35.
RX   PubMed=25381065; DOI=10.1186/1471-2474-15-371;
RA   Jeong C., Lee J.Y., Kim J., Chae H., Park H.I., Kim M., Kim O.H., Kim P.,
RA   Lee Y.K., Jung J.;
RT   "Novel COL9A3 mutation in a family diagnosed with multiple epiphyseal
RT   dysplasia: a case report.";
RL   BMC Musculoskelet. Disord. 15:371-371(2014).
RN   [13]
RP   VARIANT STL6 471-ARG--SER-684 DEL.
RX   PubMed=31090205; DOI=10.1002/ajmg.a.61191;
RA   Nixon T.R.W., Alexander P., Richards A., McNinch A., Bearcroft P.W.P.,
RA   Cobben J., Snead M.P.;
RT   "Homozygous Type IX collagen variants (COL9A1, COL9A2, and COL9A3) causing
RT   recessive Stickler syndrome-Expanding the phenotype.";
RL   Am. J. Med. Genet. A 179:1498-1506(2019).
RN   [14]
RP   VARIANTS STL6 90-ARG--SER-684 DEL AND 577-ARG--SER-684 DEL.
RX   PubMed=33570243; DOI=10.1002/mgg3.1620;
RA   Markova T., Sparber P., Borovikov A., Nagornova T., Dadali E.;
RT   "Clinical and genetic characterization of autosomal recessive stickler
RT   syndrome caused by novel compound heterozygous mutations in the COL9A3
RT   gene.";
RL   Mol. Genet. Genomic Med. 9:e1620-e1620(2021).
CC   -!- FUNCTION: Structural component of hyaline cartilage and vitreous of the
CC       eye.
CC   -!- SUBUNIT: Heterotrimer of an alpha 1(IX), an alpha 2(IX) and an alpha
CC       3(IX) chain.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- PTM: Covalently linked to the telopeptides of type II collagen by
CC       lysine-derived cross-links.
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: Multiple epiphyseal dysplasia 3 (EDM3) [MIM:600969]: A
CC       generalized skeletal dysplasia associated with significant morbidity.
CC       Joint pain, joint deformity, waddling gait, and short stature are the
CC       main clinical signs and symptoms. Radiological examination of the
CC       skeleton shows delayed, irregular mineralization of the epiphyseal
CC       ossification centers and of the centers of the carpal and tarsal bones.
CC       Multiple epiphyseal dysplasia is broadly categorized into the more
CC       severe Fairbank and the milder Ribbing types. The Fairbank type is
CC       characterized by shortness of stature, short and stubby fingers, small
CC       epiphyses in several joints, including the knee, ankle, hand, and hip.
CC       The Ribbing type is confined predominantly to the hip joints and is
CC       characterized by hands that are normal and stature that is normal or
CC       near-normal. {ECO:0000269|PubMed:10090888,
CC       ECO:0000269|PubMed:25381065}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Intervertebral disc disease (IDD) [MIM:603932]: A common
CC       musculo-skeletal disorder caused by degeneration of intervertebral
CC       disks of the lumbar spine. It results in low-back pain and unilateral
CC       leg pain. {ECO:0000269|PubMed:11308397, ECO:0000269|PubMed:25381065}.
CC       Note=Disease susceptibility is associated with variants affecting the
CC       gene represented in this entry. Susceptibility to intervertebral disk
CC       disease is conferred by variant p.Arg103Trp (PubMed:11308397).
CC       {ECO:0000269|PubMed:11308397}.
CC   -!- DISEASE: Stickler syndrome 6 (STL6) [MIM:620022]: A form of Stickler
CC       syndrome, an inherited disorder that associates ocular signs with more
CC       or less complete forms of Pierre Robin sequence, bone disorders and
CC       sensorineural deafness. Ocular disorders may include juvenile cataract,
CC       myopia, strabismus, vitreoretinal or chorioretinal degeneration,
CC       retinal detachment, and chronic uveitis. Pierre Robin sequence includes
CC       an opening in the roof of the mouth (a cleft palate), a large tongue
CC       (macroglossia), and a small lower jaw (micrognathia). Bones are
CC       affected by slight platyspondyly and large, often defective epiphyses.
CC       Juvenile joint laxity is followed by early signs of arthrosis. The
CC       degree of hearing loss varies among affected individuals and may become
CC       more severe over time. STL6 is an autosomal recessive form
CC       characterized by early-onset progressive hearing loss and progressive
CC       myopia, with variable manifestation of facial dysmorphism and skeletal
CC       anomalies. {ECO:0000269|PubMed:24273071, ECO:0000269|PubMed:30450842,
CC       ECO:0000269|PubMed:31090205, ECO:0000269|PubMed:33570243}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted
CC       helices (FACIT) family. {ECO:0000305}.
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DR   EMBL; L41162; AAC41947.1; -; mRNA.
DR   EMBL; AF026802; AAD47357.1; -; Genomic_DNA.
DR   EMBL; AF026801; AAD47357.1; JOINED; Genomic_DNA.
DR   EMBL; AL035669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC011705; AAH11705.1; -; mRNA.
DR   EMBL; X91013; CAA62495.1; -; mRNA.
DR   CCDS; CCDS13505.1; -.
DR   RefSeq; NP_001844.3; NM_001853.3.
DR   PDB; 5CTD; X-ray; 1.60 A; C=517-553.
DR   PDB; 5CTI; X-ray; 1.90 A; C=517-553.
DR   PDB; 5CVA; X-ray; 2.10 A; C/F=517-553.
DR   PDB; 5CVB; X-ray; 2.25 A; C/F=517-553.
DR   PDBsum; 5CTD; -.
DR   PDBsum; 5CTI; -.
DR   PDBsum; 5CVA; -.
DR   PDBsum; 5CVB; -.
DR   AlphaFoldDB; Q14050; -.
DR   SMR; Q14050; -.
DR   BioGRID; 107696; 7.
DR   ComplexPortal; CPX-1748; Collagen type IX trimer.
DR   IntAct; Q14050; 2.
DR   STRING; 9606.ENSP00000496793; -.
DR   GlyCosmos; Q14050; 1 site, No reported glycans.
DR   GlyGen; Q14050; 1 site.
DR   iPTMnet; Q14050; -.
DR   PhosphoSitePlus; Q14050; -.
DR   BioMuta; COL9A3; -.
DR   DMDM; 20137327; -.
DR   EPD; Q14050; -.
DR   jPOST; Q14050; -.
DR   MassIVE; Q14050; -.
DR   MaxQB; Q14050; -.
DR   PaxDb; 9606-ENSP00000341640; -.
DR   PeptideAtlas; Q14050; -.
DR   ProteomicsDB; 59803; -.
DR   Antibodypedia; 29570; 191 antibodies from 24 providers.
DR   DNASU; 1299; -.
DR   Ensembl; ENST00000649368.1; ENSP00000496793.1; ENSG00000092758.18.
DR   GeneID; 1299; -.
DR   KEGG; hsa:1299; -.
DR   MANE-Select; ENST00000649368.1; ENSP00000496793.1; NM_001853.4; NP_001844.3.
DR   UCSC; uc002ydm.3; human.
DR   AGR; HGNC:2219; -.
DR   CTD; 1299; -.
DR   DisGeNET; 1299; -.
DR   GeneCards; COL9A3; -.
DR   GeneReviews; COL9A3; -.
DR   HGNC; HGNC:2219; COL9A3.
DR   HPA; ENSG00000092758; Tissue enhanced (brain).
DR   MalaCards; COL9A3; -.
DR   MIM; 120270; gene.
DR   MIM; 600969; phenotype.
DR   MIM; 603932; phenotype.
DR   MIM; 620022; phenotype.
DR   neXtProt; NX_Q14050; -.
DR   OpenTargets; ENSG00000092758; -.
DR   Orphanet; 250984; Autosomal recessive Stickler syndrome.
DR   Orphanet; 166002; Multiple epiphyseal dysplasia due to collagen 9 anomaly.
DR   PharmGKB; PA26735; -.
DR   VEuPathDB; HostDB:ENSG00000092758; -.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00940000163687; -.
DR   HOGENOM; CLU_001074_18_2_1; -.
DR   InParanoid; Q14050; -.
DR   OMA; MINEQIA; -.
DR   OrthoDB; 5363474at2759; -.
DR   PhylomeDB; Q14050; -.
DR   PathwayCommons; Q14050; -.
DR   Reactome; R-HSA-1442490; Collagen degradation.
DR   Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-HSA-186797; Signaling by PDGF.
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-3000178; ECM proteoglycans.
DR   Reactome; R-HSA-419037; NCAM1 interactions.
DR   Reactome; R-HSA-8948216; Collagen chain trimerization.
DR   SignaLink; Q14050; -.
DR   SIGNOR; Q14050; -.
DR   BioGRID-ORCS; 1299; 16 hits in 1145 CRISPR screens.
DR   ChiTaRS; COL9A3; human.
DR   GeneWiki; COL9A3; -.
DR   GenomeRNAi; 1299; -.
DR   Pharos; Q14050; Tbio.
DR   PRO; PR:Q14050; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q14050; Protein.
DR   Bgee; ENSG00000092758; Expressed in tibia and 150 other cell types or tissues.
DR   ExpressionAtlas; Q14050; baseline and differential.
DR   GO; GO:0005594; C:collagen type IX trimer; IDA:BHF-UCL.
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: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; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   InterPro; IPR008160; Collagen.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF958; ZGC:113232; 1.
DR   Pfam; PF01391; Collagen; 5.
DR   Genevisible; Q14050; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Collagen; Deafness; Disease variant; Dwarfism;
KW   Extracellular matrix; Glycoprotein; Hydroxylation; Reference proteome;
KW   Repeat; Secreted; Signal; Stickler syndrome.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..684
FT                   /note="Collagen alpha-3(IX) chain"
FT                   /id="PRO_0000005848"
FT   REGION          26..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          29..519
FT                   /note="Triple-helical region 3 (COL3)"
FT   REGION          520..550
FT                   /note="Nonhelical region 3 (NC3)"
FT   REGION          548..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..630
FT                   /note="Triple-helical region 2 (COL2)"
FT   REGION          631..632
FT                   /note="Nonhelical region 2 (NC2)"
FT   REGION          633..661
FT                   /note="Triple-helical region 1 (COL1)"
FT   REGION          662..684
FT                   /note="Nonhelical region 1 (NC1)"
FT   MOTIF           423..425
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           601..603
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        54..68
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..163
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..190
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..574
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        483
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         35
FT                   /note="G -> D (in EDM3; dbSNP:rs1390736361)"
FT                   /evidence="ECO:0000269|PubMed:25381065"
FT                   /id="VAR_072736"
FT   VARIANT         90..684
FT                   /note="Missing (in STL6)"
FT                   /evidence="ECO:0000269|PubMed:33570243"
FT                   /id="VAR_087540"
FT   VARIANT         94
FT                   /note="P -> S (in dbSNP:rs35908728)"
FT                   /id="VAR_048808"
FT   VARIANT         103
FT                   /note="R -> Q (in dbSNP:rs142639450)"
FT                   /evidence="ECO:0000269|PubMed:11565064"
FT                   /id="VAR_026467"
FT   VARIANT         103
FT                   /note="R -> W (probable risk factor for intervertebral disk
FT                   disease; dbSNP:rs61734651)"
FT                   /evidence="ECO:0000269|PubMed:11565064"
FT                   /id="VAR_026468"
FT   VARIANT         296
FT                   /note="P -> L (in dbSNP:rs45628843)"
FT                   /evidence="ECO:0000269|PubMed:11565064"
FT                   /id="VAR_026469"
FT   VARIANT         402
FT                   /note="R -> Q (in dbSNP:rs373519549)"
FT                   /evidence="ECO:0000269|PubMed:11565064"
FT                   /id="VAR_026470"
FT   VARIANT         435
FT                   /note="A -> E (in dbSNP:rs751557)"
FT                   /evidence="ECO:0000269|PubMed:11565064,
FT                   ECO:0000269|PubMed:8586434"
FT                   /id="VAR_026471"
FT   VARIANT         471..684
FT                   /note="Missing (in STL6)"
FT                   /evidence="ECO:0000269|PubMed:31090205"
FT                   /id="VAR_087541"
FT   VARIANT         563..565
FT                   /note="Missing"
FT                   /evidence="ECO:0000269|PubMed:10428822"
FT                   /id="VAR_012660"
FT   VARIANT         564..566
FT                   /note="Missing"
FT                   /evidence="ECO:0000269|PubMed:10428822"
FT                   /id="VAR_012661"
FT   VARIANT         577..684
FT                   /note="Missing (in STL6)"
FT                   /evidence="ECO:0000269|PubMed:33570243"
FT                   /id="VAR_087542"
FT   CONFLICT        18
FT                   /note="E -> Q (in Ref. 1; AAC41947 and 2; AAD47357)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        39
FT                   /note="P -> R (in Ref. 1; AAC41947)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        144
FT                   /note="S -> P (in Ref. 1; AAC41947)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        524
FT                   /note="R -> H (in Ref. 5; CAA62495)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        576
FT                   /note="A -> T (in Ref. 5; CAA62495)"
FT                   /evidence="ECO:0000305"
FT   HELIX           522..543
FT                   /evidence="ECO:0007829|PDB:5CTD"
SQ   SEQUENCE   684 AA;  63616 MW;  892F035CF6E06733 CRC64;
     MAGPRACAPL LLLLLLGELL AAAGAQRVGL PGPPGPPGPP GKPGQDGIDG EAGPPGLPGP
     PGPKGAPGKP GKPGEAGLPG LPGVDGLTGR DGPPGPKGAP GERGSLGPPG PPGLGGKGLP
     GPPGEAGVSG PPGGIGLRGP PGPSGLPGLP GPPGPPGPPG HPGVLPEGAT DLQCPSICPP
     GPPGPPGMPG FKGPTGYKGE QGEVGKDGEK GDPGPPGPAG LPGSVGLQGP RGLRGLPGPL
     GPPGDRGPIG FRGPPGIPGA PGKAGDRGER GPEGFRGPKG DLGRPGPKGT PGVAGPSGEP
     GMPGKDGQNG VPGLDGQKGE AGRNGAPGEK GPNGLPGLPG RAGSKGEKGE RGRAGELGEA
     GPSGEPGVPG DAGMPGERGE AGHRGSAGAL GPQGPPGAPG VRGFQGQKGS MGDPGLPGPQ
     GLRGDVGDRG PGGAAGPKGD QGIAGSDGLP GDKGELGPSG LVGPKGESGS RGELGPKGTQ
     GPNGTSGVQG VPGPPGPLGL QGVPGVPGIT GKPGVPGKEA SEQRIRELCG GMISEQIAQL
     AAHLRKPLAP GSIGRPGPAG PPGPPGPPGS IGHPGARGPP GYRGPTGELG DPGPRGNQGD
     RGDKGAAGAG LDGPEGDQGP QGPQGVPGTS KDGQDGAPGE PGPPGDPGLP GAIGAQGTPG
     ICDTSACQGA VLGGVGEKSG SRSS
//