S26A2_HUMAN
ID S26A2_HUMAN Reviewed; 739 AA.
AC P50443; A8K2U3; B2R6J1; Q6N051;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Sulfate transporter;
DE AltName: Full=Diastrophic dysplasia protein;
DE AltName: Full=Solute carrier family 26 member 2;
GN Name=SLC26A2; Synonyms=DTD, DTDST;
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], VARIANT THR-574, FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=7923357; DOI=10.1016/0092-8674(94)90281-x;
RA Haestbacka J., de la Chapelle A., Mahtani M.M., Clines G., Reeve-Daly M.P.,
RA Daly M., Hamilton B.A., Kusumi K., Trivedi B., Weaver A., Coloma A.,
RA Lovett M., Buckler A., Kaitila I., Lander E.S.;
RT "The diastrophic dysplasia gene encodes a novel sulfate transporter:
RT positional cloning by fine-structure linkage disequilibrium mapping.";
RL Cell 78:1073-1087(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-574.
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-574.
RC TISSUE=Placenta;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 614-739.
RC TISSUE=Prostate;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-16, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP VARIANTS ACG1B VAL-340 DEL; ASP-425 AND VAL-678.
RX PubMed=8528239; DOI=10.1038/ng0196-100;
RA Superti-Furga A., Haestbacka J., Wilcox W.R., Cohn D.H.,
RA van der Harten H.J., Rossi A., Blau N., Rimoin D.L., Steinmann B.,
RA Lander E.S., Gitzelmann R.;
RT "Achondrogenesis type IB is caused by mutations in the diastrophic
RT dysplasia sulphate transporter gene.";
RL Nat. Genet. 12:100-102(1996).
RN [9]
RP VARIANTS AO2 GLU-255; TRP-279 AND VAL-715.
RX PubMed=8571951;
RA Haestbacka J., Superti-Furga A., Wilcox W.R., Rimoin D.L., Cohn D.H.,
RA Lander E.S.;
RT "Atelosteogenesis type II is caused by mutations in the diastrophic
RT dysplasia sulfate-transporter gene (DTDST): evidence for a phenotypic
RT series involving three chondrodysplasias.";
RL Am. J. Hum. Genet. 58:255-262(1996).
RN [10]
RP VARIANT DIATROPHIC DYSPLASIA PRO-454.
RX PubMed=10466420; DOI=10.1034/j.1399-0004.1999.560110.x;
RA Megarbane A., Haddad F.A., Haddad-Zebouni S., Achram M., Eich G.,
RA Le Merrer M., Superti-Furga A.;
RT "Homozygosity for a novel DTDST mutation in a child with a 'broad bone-
RT platyspondylic' variant of diastrophic dysplasia.";
RL Clin. Genet. 56:71-76(1999).
RN [11]
RP VARIANT EDM4 SER-653.
RX PubMed=12966518; DOI=10.1002/ajmg.a.20282;
RA Maekitie O., Savarirayan R., Bonafe L., Robertson S., Susic M.,
RA Superti-Furga A., Cole W.G.;
RT "Autosomal recessive multiple epiphyseal dysplasia with homozygosity for
RT C653S in the DTDST gene: double-layer patella as a reliable sign.";
RL Am. J. Med. Genet. A 122:187-192(2003).
RN [12]
RP VARIANTS EDM4 SER-256; TRP-279; SER-653 AND VAL-715.
RX PubMed=21922596; DOI=10.1002/humu.21611;
RA Jackson G.C., Mittaz-Crettol L., Taylor J.A., Mortier G.R., Spranger J.,
RA Zabel B., Le Merrer M., Cormier-Daire V., Hall C.M., Offiah A.,
RA Wright M.J., Savarirayan R., Nishimura G., Ramsden S.C., Elles R.,
RA Bonafe L., Superti-Furga A., Unger S., Zankl A., Briggs M.D.;
RT "Pseudoachondroplasia and multiple epiphyseal dysplasia: A 7-year
RT comprehensive analysis of the known disease genes identify novel and
RT recurrent mutations and provides an accurate assessment of their relative
RT contribution.";
RL Hum. Mutat. 33:144-157(2012).
CC -!- FUNCTION: Sulfate transporter. May play a role in endochondral bone
CC formation. {ECO:0000269|PubMed:7923357}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7923357};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:7923357}.
CC -!- DISEASE: Diastrophic dysplasia (DTD) [MIM:222600]: An autosomal
CC recessive disease characterized by osteochondrodysplasia with clinical
CC features including dwarfism, spinal deformation, and specific joint
CC abnormalities. {ECO:0000269|PubMed:10466420}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Achondrogenesis 1B (ACG1B) [MIM:600972]: A form of
CC achondrogenesis type 1, a lethal form of chondrodysplasia characterized
CC by deficient ossification in the lumbar vertebrae and absent
CC ossification in the sacral, pubic and ischial bones and clinically by
CC stillbirth or early death. In addition to severe micromelia, there is a
CC disproportionately large cranium due to marked edema of soft tissues.
CC ACG1B is an autosomal recessive disease. {ECO:0000269|PubMed:8528239}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Atelosteogenesis 2 (AO2) [MIM:256050]: A perinatal dysplasia
CC characterized by shortening of the limbs, a dysmorphic syndrome and
CC radiographic skeletal features. Patients are stillborn or die soon
CC after birth. {ECO:0000269|PubMed:8571951}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- DISEASE: Multiple epiphyseal dysplasia 4 (EDM4) [MIM:226900]: 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. Multiple epiphyseal dysplasia type 4 is a recessively
CC inherited form, characterized by early childhood-onset hip dysplasia
CC and recurrent patella dislocation. Short stature is not frequent.
CC {ECO:0000269|PubMed:12966518, ECO:0000269|PubMed:21922596}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000305}.
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DR EMBL; U14528; AAA70081.1; -; mRNA.
DR EMBL; AK290358; BAF83047.1; -; mRNA.
DR EMBL; AK312596; BAG35488.1; -; mRNA.
DR EMBL; AC008427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61755.1; -; Genomic_DNA.
DR EMBL; BC059390; AAH59390.1; -; mRNA.
DR EMBL; BX640696; CAE45819.1; -; mRNA.
DR CCDS; CCDS4300.1; -.
DR PIR; A54808; A54808.
DR RefSeq; NP_000103.2; NM_000112.3.
DR RefSeq; XP_016864680.1; XM_017009191.1.
DR AlphaFoldDB; P50443; -.
DR SMR; P50443; -.
DR BioGRID; 108169; 56.
DR IntAct; P50443; 14.
DR STRING; 9606.ENSP00000286298; -.
DR TCDB; 2.A.53.2.1; the sulfate permease (sulp) family.
DR GlyGen; P50443; 3 sites.
DR iPTMnet; P50443; -.
DR PhosphoSitePlus; P50443; -.
DR SwissPalm; P50443; -.
DR BioMuta; SLC26A2; -.
DR DMDM; 254763328; -.
DR EPD; P50443; -.
DR jPOST; P50443; -.
DR MassIVE; P50443; -.
DR MaxQB; P50443; -.
DR PaxDb; P50443; -.
DR PeptideAtlas; P50443; -.
DR PRIDE; P50443; -.
DR ProteomicsDB; 56225; -.
DR Antibodypedia; 27892; 150 antibodies from 24 providers.
DR DNASU; 1836; -.
DR Ensembl; ENST00000286298.5; ENSP00000286298.4; ENSG00000155850.9.
DR GeneID; 1836; -.
DR KEGG; hsa:1836; -.
DR MANE-Select; ENST00000286298.5; ENSP00000286298.4; NM_000112.4; NP_000103.2.
DR UCSC; uc003lrh.4; human.
DR CTD; 1836; -.
DR DisGeNET; 1836; -.
DR GeneCards; SLC26A2; -.
DR GeneReviews; SLC26A2; -.
DR HGNC; HGNC:10994; SLC26A2.
DR HPA; ENSG00000155850; Tissue enriched (intestine).
DR MalaCards; SLC26A2; -.
DR MIM; 222600; phenotype.
DR MIM; 226900; phenotype.
DR MIM; 256050; phenotype.
DR MIM; 600972; phenotype.
DR MIM; 606718; gene.
DR neXtProt; NX_P50443; -.
DR OpenTargets; ENSG00000155850; -.
DR Orphanet; 93298; Achondrogenesis type 1B.
DR Orphanet; 56304; Atelosteogenesis type II.
DR Orphanet; 628; Diastrophic dysplasia.
DR Orphanet; 93307; Multiple epiphyseal dysplasia type 4.
DR PharmGKB; PA149; -.
DR VEuPathDB; HostDB:ENSG00000155850; -.
DR eggNOG; KOG0236; Eukaryota.
DR GeneTree; ENSGT01050000244925; -.
DR HOGENOM; CLU_003182_9_4_1; -.
DR InParanoid; P50443; -.
DR OMA; ALYWIPK; -.
DR OrthoDB; 690428at2759; -.
DR PhylomeDB; P50443; -.
DR TreeFam; TF313784; -.
DR PathwayCommons; P50443; -.
DR Reactome; R-HSA-174362; Transport and synthesis of PAPS.
DR Reactome; R-HSA-3560792; Defective SLC26A2 causes chondrodysplasias.
DR Reactome; R-HSA-427601; Multifunctional anion exchangers.
DR SignaLink; P50443; -.
DR BioGRID-ORCS; 1836; 9 hits in 1080 CRISPR screens.
DR ChiTaRS; SLC26A2; human.
DR GeneWiki; SLC26A2; -.
DR GenomeRNAi; 1836; -.
DR Pharos; P50443; Tbio.
DR PRO; PR:P50443; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P50443; protein.
DR Bgee; ENSG00000155850; Expressed in colonic mucosa and 200 other tissues.
DR ExpressionAtlas; P50443; baseline and differential.
DR Genevisible; P50443; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0031528; C:microvillus membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0015301; F:anion:anion antiporter activity; IBA:GO_Central.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0019531; F:oxalate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0050428; P:3'-phosphoadenosine 5'-phosphosulfate biosynthetic process; TAS:Reactome.
DR GO; GO:0006811; P:ion transport; TAS:Reactome.
DR GO; GO:0001503; P:ossification; IEA:Ensembl.
DR GO; GO:1902358; P:sulfate transmembrane transport; IMP:UniProtKB.
DR Gene3D; 3.30.750.24; -; 1.
DR InterPro; IPR018045; S04_transporter_CS.
DR InterPro; IPR011547; SLC26A/SulP_dom.
DR InterPro; IPR001902; SLC26A/SulP_fam.
DR InterPro; IPR030280; SLC26A2.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR PANTHER; PTHR11814; PTHR11814; 1.
DR PANTHER; PTHR11814:SF16; PTHR11814:SF16; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SUPFAM; SSF52091; SSF52091; 1.
DR TIGRFAMs; TIGR00815; sulP; 1.
DR PROSITE; PS01130; SLC26A; 1.
DR PROSITE; PS50801; STAS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disease variant; Dwarfism; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..739
FT /note="Sulfate transporter"
FT /id="PRO_0000080158"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 568..719
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 255
FT /note="G -> E (in AO2; dbSNP:rs104893917)"
FT /evidence="ECO:0000269|PubMed:8571951"
FT /id="VAR_007434"
FT VARIANT 256
FT /note="F -> S (in EDM4; dbSNP:rs1419613966)"
FT /evidence="ECO:0000269|PubMed:21922596"
FT /id="VAR_066835"
FT VARIANT 279
FT /note="R -> W (in AO2 and EDM4; dbSNP:rs104893915)"
FT /evidence="ECO:0000269|PubMed:21922596,
FT ECO:0000269|PubMed:8571951"
FT /id="VAR_007435"
FT VARIANT 340
FT /note="Missing (in ACG1B)"
FT /evidence="ECO:0000269|PubMed:8528239"
FT /id="VAR_007436"
FT VARIANT 425
FT /note="N -> D (in ACG1B; dbSNP:rs104893920)"
FT /evidence="ECO:0000269|PubMed:8528239"
FT /id="VAR_007437"
FT VARIANT 454
FT /note="Q -> P (in diatrophic dysplasia; broad bone-
FT platyspondylic variant; dbSNP:rs104893921)"
FT /evidence="ECO:0000269|PubMed:10466420"
FT /id="VAR_018654"
FT VARIANT 574
FT /note="I -> T (in dbSNP:rs30832)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7923357"
FT /id="VAR_058415"
FT VARIANT 653
FT /note="C -> S (in EDM4; dbSNP:rs104893924)"
FT /evidence="ECO:0000269|PubMed:12966518,
FT ECO:0000269|PubMed:21922596"
FT /id="VAR_018655"
FT VARIANT 678
FT /note="G -> V (in ACG1B; dbSNP:rs104893916)"
FT /evidence="ECO:0000269|PubMed:8528239"
FT /id="VAR_007438"
FT VARIANT 689
FT /note="T -> S (in dbSNP:rs3776070)"
FT /id="VAR_020402"
FT VARIANT 715
FT /note="A -> V (in AO2 and EDM4; dbSNP:rs104893918)"
FT /evidence="ECO:0000269|PubMed:21922596,
FT ECO:0000269|PubMed:8571951"
FT /id="VAR_007439"
FT CONFLICT 619
FT /note="R -> G (in Ref. 6; CAE45819)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="K -> R (in Ref. 2; BAG35488)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 739 AA; 81662 MW; 577984D0E973087F CRC64;
MSSESKEQHN VSPRDSAEGN DSYPSGIHLE LQRESSTDFK QFETNDQCRP YHRILIERQE
KSDTNFKEFV IKKLQKNCQC SPAKAKNMIL GFLPVLQWLP KYDLKKNILG DVMSGLIVGI
LLVPQSIAYS LLAGQEPVYG LYTSFFASII YFLLGTSRHI SVGIFGVLCL MIGETVDREL
QKAGYDNAHS APSLGMVSNG STLLNHTSDR ICDKSCYAIM VGSTVTFIAG VYQVAMGFFQ
VGFVSVYLSD ALLSGFVTGA SFTILTSQAK YLLGLNLPRT NGVGSLITTW IHVFRNIHKT
NLCDLITSLL CLLVLLPTKE LNEHFKSKLK APIPIELVVV VAATLASHFG KLHENYNSSI
AGHIPTGFMP PKVPEWNLIP SVAVDAIAIS IIGFAITVSL SEMFAKKHGY TVKANQEMYA
IGFCNIIPSF FHCFTTSAAL AKTLVKESTG CHTQLSGVVT ALVLLLVLLV IAPLFYSLQK
SVLGVITIVN LRGALRKFRD LPKMWSISRM DTVIWFVTML SSALLSTEIG LLVGVCFSIF
CVILRTQKPK SSLLGLVEES EVFESVSAYK NLQIKPGIKI FRFVAPLYYI NKECFKSALY
KQTVNPILIK VAWKKAAKRK IKEKVVTLGG IQDEMSVQLS HDPLELHTIV IDCSAIQFLD
TAGIHTLKEV RRDYEAIGIQ VLLAQCNPTV RDSLTNGEYC KKEEENLLFY SVYEAMAFAE
VSKNQKGVCV PNGLSLSSD
