Full text data of SLC25A16
SLC25A16
(GDA)
[Confidence: low (only semi-automatic identification from reviews)]
Graves disease carrier protein; GDC (Graves disease autoantigen; GDA; Mitochondrial solute carrier protein homolog; Solute carrier family 25 member 16)
Graves disease carrier protein; GDC (Graves disease autoantigen; GDA; Mitochondrial solute carrier protein homolog; Solute carrier family 25 member 16)
UniProt
P16260
ID GDC_HUMAN Reviewed; 332 AA.
AC P16260; Q8N2U1;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 25-NOV-2008, sequence version 3.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=Graves disease carrier protein;
DE Short=GDC;
DE AltName: Full=Graves disease autoantigen;
DE Short=GDA;
DE AltName: Full=Mitochondrial solute carrier protein homolog;
DE AltName: Full=Solute carrier family 25 member 16;
GN Name=SLC25A16; Synonyms=GDA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thyroid;
RX PubMed=2575220;
RA Zarrilli R., Oates E.L., McBride O.W., Lerman M.I., Chan J.Y.,
RA Santisteban P., Ursini M.V., Notkins A.L., Kohn L.D.;
RT "Sequence and chromosomal assignment of a novel cDNA identified by
RT immunoscreening of a thyroid expression library: similarity to a
RT family of mitochondrial solute carrier proteins.";
RL Mol. Endocrinol. 3:1498-1505(1989).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RX PubMed=1457817;
RA Fiermonte G., Runswick M.J., Walker J.E., Palmieri F.;
RT "Sequence and pattern of expression of a bovine homologue of a human
RT mitochondrial transport protein associated with Grave's disease.";
RL DNA Seq. 3:71-78(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11158296; DOI=10.1128/MCB.21.4.1089-1097.2001;
RA Prohl C., Pelzer W., Diekert K., Kmita H., Bedekovics T., Kispal G.,
RA Lill R.;
RT "The yeast mitochondrial carrier Leu5p and its human homologue Graves'
RT disease protein are required for accumulation of coenzyme A in the
RT matrix.";
RL Mol. Cell. Biol. 21:1089-1097(2001).
RN [8]
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).
CC -!- FUNCTION: Required for the accumulation of coenzyme A in the
CC mitochondrial matrix.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC membrane protein.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29)
CC family.
CC -!- SIMILARITY: Contains 3 Solcar repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36329.1; Type=Frameshift; Positions=320;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M31659; AAA36329.1; ALT_FRAME; mRNA.
DR EMBL; AK290255; BAF82944.1; -; mRNA.
DR EMBL; AL713888; CAI15116.1; -; Genomic_DNA.
DR EMBL; CH471083; EAW54298.1; -; Genomic_DNA.
DR EMBL; BC030266; AAH30266.1; -; mRNA.
DR PIR; A40141; A40141.
DR RefSeq; NP_689920.1; NM_152707.3.
DR UniGene; Hs.180408; -.
DR ProteinModelPortal; P16260; -.
DR SMR; P16260; 36-327.
DR STRING; 9606.ENSP00000265870; -.
DR TCDB; 2.A.29.12.3; the mitochondrial carrier (mc) family.
DR PhosphoSite; P16260; -.
DR DMDM; 215274156; -.
DR PaxDb; P16260; -.
DR PRIDE; P16260; -.
DR DNASU; 8034; -.
DR Ensembl; ENST00000265870; ENSP00000265870; ENSG00000122912.
DR GeneID; 8034; -.
DR KEGG; hsa:8034; -.
DR UCSC; uc001joi.3; human.
DR CTD; 8034; -.
DR GeneCards; GC10M070242; -.
DR HGNC; HGNC:10986; SLC25A16.
DR HPA; HPA044580; -.
DR MIM; 139080; gene.
DR neXtProt; NX_P16260; -.
DR PharmGKB; PA35862; -.
DR eggNOG; NOG274055; -.
DR HOGENOM; HOG000165726; -.
DR HOVERGEN; HBG104402; -.
DR InParanoid; P16260; -.
DR KO; K15084; -.
DR OMA; KTHVNLL; -.
DR OrthoDB; EOG7HXCR5; -.
DR PhylomeDB; P16260; -.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR GenomeRNAi; 8034; -.
DR NextBio; 30619; -.
DR PRO; PR:P16260; -.
DR ArrayExpress; P16260; -.
DR Bgee; P16260; -.
DR CleanEx; HS_GDA; -.
DR CleanEx; HS_SLC25A16; -.
DR Genevestigator; P16260; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; NAS:UniProtKB.
DR GO; GO:0015297; F:antiporter activity; NAS:UniProtKB.
DR GO; GO:0009108; P:coenzyme biosynthetic process; TAS:Reactome.
DR GO; GO:0015939; P:pantothenate metabolic process; TAS:Reactome.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR002167; Graves_DC.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00928; GRAVESDC.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Complete proteome; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 332 Graves disease carrier protein.
FT /FTId=PRO_0000090616.
FT TRANSMEM 37 57 Helical; Name=1; (Potential).
FT TRANSMEM 88 108 Helical; Name=2; (Potential).
FT TRANSMEM 134 154 Helical; Name=3; (Potential).
FT TRANSMEM 191 211 Helical; Name=4; (Potential).
FT TRANSMEM 244 264 Helical; Name=5; (Potential).
FT TRANSMEM 299 319 Helical; Name=6; (Potential).
FT REPEAT 34 120 Solcar 1.
FT REPEAT 128 216 Solcar 2.
FT REPEAT 238 328 Solcar 3.
FT CONFLICT 21 21 Q -> G (in Ref. 1; AAA36329).
FT CONFLICT 44 44 G -> S (in Ref. 1; AAA36329).
FT CONFLICT 149 151 YPL -> DPV (in Ref. 1; AAA36329).
FT CONFLICT 167 167 S -> R (in Ref. 1; AAA36329).
FT CONFLICT 227 227 R -> S (in Ref. 1; AAA36329).
FT CONFLICT 251 251 G -> R (in Ref. 1; AAA36329).
FT CONFLICT 290 290 V -> D (in Ref. 1; AAA36329).
SQ SEQUENCE 332 AA; 36224 MW; 71C2C3D413F80246 CRC64;
MAAATAAAAL AAADPPPAMP QAAGAGGPTT RRDFYWLRSF LAGGIAGCCA KTTVAPLDRV
KVLLQAHNHH YKHLGVFSAL RAVPQKEGFL GLYKGNGAMM IRIFPYGAIQ FMAFEHYKTL
ITTKLGISGH VHRLMAGSMA GMTAVICTYP LDMVRVRLAF QVKGEHSYTG IIHAFKTIYA
KEGGFFGFYR GLMPTILGMA PYAGVSFFTF GTLKSVGLSH APTLLGRPSS DNPNVLVLKT
HVNLLCGGVA GAIAQTISYP FDVTRRRMQL GTVLPEFEKC LTMRDTMKYV YGHHGIRKGL
YRGLSLNYIR CIPSQAVAFT TYELMKQFFH LN
//
ID GDC_HUMAN Reviewed; 332 AA.
AC P16260; Q8N2U1;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 25-NOV-2008, sequence version 3.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=Graves disease carrier protein;
DE Short=GDC;
DE AltName: Full=Graves disease autoantigen;
DE Short=GDA;
DE AltName: Full=Mitochondrial solute carrier protein homolog;
DE AltName: Full=Solute carrier family 25 member 16;
GN Name=SLC25A16; Synonyms=GDA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thyroid;
RX PubMed=2575220;
RA Zarrilli R., Oates E.L., McBride O.W., Lerman M.I., Chan J.Y.,
RA Santisteban P., Ursini M.V., Notkins A.L., Kohn L.D.;
RT "Sequence and chromosomal assignment of a novel cDNA identified by
RT immunoscreening of a thyroid expression library: similarity to a
RT family of mitochondrial solute carrier proteins.";
RL Mol. Endocrinol. 3:1498-1505(1989).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RX PubMed=1457817;
RA Fiermonte G., Runswick M.J., Walker J.E., Palmieri F.;
RT "Sequence and pattern of expression of a bovine homologue of a human
RT mitochondrial transport protein associated with Grave's disease.";
RL DNA Seq. 3:71-78(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11158296; DOI=10.1128/MCB.21.4.1089-1097.2001;
RA Prohl C., Pelzer W., Diekert K., Kmita H., Bedekovics T., Kispal G.,
RA Lill R.;
RT "The yeast mitochondrial carrier Leu5p and its human homologue Graves'
RT disease protein are required for accumulation of coenzyme A in the
RT matrix.";
RL Mol. Cell. Biol. 21:1089-1097(2001).
RN [8]
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).
CC -!- FUNCTION: Required for the accumulation of coenzyme A in the
CC mitochondrial matrix.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC membrane protein.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29)
CC family.
CC -!- SIMILARITY: Contains 3 Solcar repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36329.1; Type=Frameshift; Positions=320;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M31659; AAA36329.1; ALT_FRAME; mRNA.
DR EMBL; AK290255; BAF82944.1; -; mRNA.
DR EMBL; AL713888; CAI15116.1; -; Genomic_DNA.
DR EMBL; CH471083; EAW54298.1; -; Genomic_DNA.
DR EMBL; BC030266; AAH30266.1; -; mRNA.
DR PIR; A40141; A40141.
DR RefSeq; NP_689920.1; NM_152707.3.
DR UniGene; Hs.180408; -.
DR ProteinModelPortal; P16260; -.
DR SMR; P16260; 36-327.
DR STRING; 9606.ENSP00000265870; -.
DR TCDB; 2.A.29.12.3; the mitochondrial carrier (mc) family.
DR PhosphoSite; P16260; -.
DR DMDM; 215274156; -.
DR PaxDb; P16260; -.
DR PRIDE; P16260; -.
DR DNASU; 8034; -.
DR Ensembl; ENST00000265870; ENSP00000265870; ENSG00000122912.
DR GeneID; 8034; -.
DR KEGG; hsa:8034; -.
DR UCSC; uc001joi.3; human.
DR CTD; 8034; -.
DR GeneCards; GC10M070242; -.
DR HGNC; HGNC:10986; SLC25A16.
DR HPA; HPA044580; -.
DR MIM; 139080; gene.
DR neXtProt; NX_P16260; -.
DR PharmGKB; PA35862; -.
DR eggNOG; NOG274055; -.
DR HOGENOM; HOG000165726; -.
DR HOVERGEN; HBG104402; -.
DR InParanoid; P16260; -.
DR KO; K15084; -.
DR OMA; KTHVNLL; -.
DR OrthoDB; EOG7HXCR5; -.
DR PhylomeDB; P16260; -.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR GenomeRNAi; 8034; -.
DR NextBio; 30619; -.
DR PRO; PR:P16260; -.
DR ArrayExpress; P16260; -.
DR Bgee; P16260; -.
DR CleanEx; HS_GDA; -.
DR CleanEx; HS_SLC25A16; -.
DR Genevestigator; P16260; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; NAS:UniProtKB.
DR GO; GO:0015297; F:antiporter activity; NAS:UniProtKB.
DR GO; GO:0009108; P:coenzyme biosynthetic process; TAS:Reactome.
DR GO; GO:0015939; P:pantothenate metabolic process; TAS:Reactome.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR002167; Graves_DC.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00928; GRAVESDC.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Complete proteome; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 332 Graves disease carrier protein.
FT /FTId=PRO_0000090616.
FT TRANSMEM 37 57 Helical; Name=1; (Potential).
FT TRANSMEM 88 108 Helical; Name=2; (Potential).
FT TRANSMEM 134 154 Helical; Name=3; (Potential).
FT TRANSMEM 191 211 Helical; Name=4; (Potential).
FT TRANSMEM 244 264 Helical; Name=5; (Potential).
FT TRANSMEM 299 319 Helical; Name=6; (Potential).
FT REPEAT 34 120 Solcar 1.
FT REPEAT 128 216 Solcar 2.
FT REPEAT 238 328 Solcar 3.
FT CONFLICT 21 21 Q -> G (in Ref. 1; AAA36329).
FT CONFLICT 44 44 G -> S (in Ref. 1; AAA36329).
FT CONFLICT 149 151 YPL -> DPV (in Ref. 1; AAA36329).
FT CONFLICT 167 167 S -> R (in Ref. 1; AAA36329).
FT CONFLICT 227 227 R -> S (in Ref. 1; AAA36329).
FT CONFLICT 251 251 G -> R (in Ref. 1; AAA36329).
FT CONFLICT 290 290 V -> D (in Ref. 1; AAA36329).
SQ SEQUENCE 332 AA; 36224 MW; 71C2C3D413F80246 CRC64;
MAAATAAAAL AAADPPPAMP QAAGAGGPTT RRDFYWLRSF LAGGIAGCCA KTTVAPLDRV
KVLLQAHNHH YKHLGVFSAL RAVPQKEGFL GLYKGNGAMM IRIFPYGAIQ FMAFEHYKTL
ITTKLGISGH VHRLMAGSMA GMTAVICTYP LDMVRVRLAF QVKGEHSYTG IIHAFKTIYA
KEGGFFGFYR GLMPTILGMA PYAGVSFFTF GTLKSVGLSH APTLLGRPSS DNPNVLVLKT
HVNLLCGGVA GAIAQTISYP FDVTRRRMQL GTVLPEFEKC LTMRDTMKYV YGHHGIRKGL
YRGLSLNYIR CIPSQAVAFT TYELMKQFFH LN
//
MIM
139080
*RECORD*
*FIELD* NO
139080
*FIELD* TI
*139080 SOLUTE CARRIER FAMILY 25 (MITOCHONDRIAL CARRIER, GRAVES DISEASE AUTOANTIGEN),
read moreMEMBER 16; SLC25A16
;;GRAVES DISEASE AUTOANTIGEN; GDA;;
D10S105E
*FIELD* TX
By screening a human thyroid expression library with antibody-rich sera
from patients with Graves disease (275000), Zarrilli et al. (1989)
isolated a cDNA clone, which they termed hGT, that was reactive with
most of the sera. The predicted amino acid sequence of 348 residues
exhibited a strong homology with the mitochondrial ADP/ATP carrier
protein (ADP/ATP translocator). (Three ADP/ATP translocator proteins are
located on chromosome 4 (103220) and on the X chromosome (300150,
300151).)
By somatic cell hybrid analysis, Zarrilli et al. (1989) mapped the
Graves disease autoantigen to chromosome 10. Using the cDNA isolated by
Zarrilli et al. (1989) as a probe, Rossi et al. (1993) further localized
the GDA gene to 10q21.3-q22.1 by nonisotopic in situ hybridization.
Mitochondrial carrier proteins, which are localized in the inner
membrane, facilitate the rapid transport and exchange of molecules
between the cytosol and the mitochondrial matrix space. SLC25A16 is 35%
identical to the yeast mitochondrial carrier protein Leu5. In yeast
strains lacking Leu5, Prohl et al. (2001) detected reduced
mitochondrial, but not cytosolic, CoA levels. Organelles from
Leu5-negative cells were not capable of synthesis of
alpha-isopropylmalate (IPM) because the IPM synthase was trapped in the
mitochondria. Mutant yeast also lacked peroxisomal citrate synthase.
Transformation of mutant yeast cells with a plasmid carrying SLC25A16 at
least partially replaced Leu5 function, suggesting a role for SLC25A16
in mitochondrial function.
*FIELD* RF
1. Prohl, C.; Pelzer, W.; Diekert, K.; Kmita, H.; Bedekovics, T.;
Kispal, G.; Lill, R.: The yeast mitochondrial carrier Leu5p and its
human homologue Graves' disease protein are required for accumulation
of coenzyme A in the matrix. Molec. Cell Biol. 21: 1089-1097, 2001.
2. Rossi, E.; Zarrilli, R.; Zuffardi, O.: Regional assignment of
the gene coding for a human Graves' disease autoantigen to 10q21.3-q22.1. Hum.
Genet. 90: 653-654, 1993.
3. Zarrilli, R.; Oates, E. L.; McBride, O. W.; Lerman, M. I.; Chan,
J. Y.; Santisteban, P.; Ursini, M. V.; Notkins, A. L.; Kohn, L. D.
: Sequence and chromosomal assignment of a novel cDNA identified by
immunoscreening of a thyroid expression library: similarity to a family
of mitochondrial solute carrier proteins. Molec. Endocr. 3: 1498-1508,
1989.
*FIELD* CD
Victor A. McKusick: 4/27/1993
*FIELD* ED
cwells: 11/12/2003
mgross: 5/11/2001
mcapotos: 5/11/2001
mcapotos: 5/10/2001
psherman: 7/29/1999
psherman: 7/23/1998
mark: 6/5/1996
terry: 6/3/1996
mimadm: 9/24/1994
carol: 5/16/1994
carol: 10/26/1993
carol: 4/27/1993
*RECORD*
*FIELD* NO
139080
*FIELD* TI
*139080 SOLUTE CARRIER FAMILY 25 (MITOCHONDRIAL CARRIER, GRAVES DISEASE AUTOANTIGEN),
read moreMEMBER 16; SLC25A16
;;GRAVES DISEASE AUTOANTIGEN; GDA;;
D10S105E
*FIELD* TX
By screening a human thyroid expression library with antibody-rich sera
from patients with Graves disease (275000), Zarrilli et al. (1989)
isolated a cDNA clone, which they termed hGT, that was reactive with
most of the sera. The predicted amino acid sequence of 348 residues
exhibited a strong homology with the mitochondrial ADP/ATP carrier
protein (ADP/ATP translocator). (Three ADP/ATP translocator proteins are
located on chromosome 4 (103220) and on the X chromosome (300150,
300151).)
By somatic cell hybrid analysis, Zarrilli et al. (1989) mapped the
Graves disease autoantigen to chromosome 10. Using the cDNA isolated by
Zarrilli et al. (1989) as a probe, Rossi et al. (1993) further localized
the GDA gene to 10q21.3-q22.1 by nonisotopic in situ hybridization.
Mitochondrial carrier proteins, which are localized in the inner
membrane, facilitate the rapid transport and exchange of molecules
between the cytosol and the mitochondrial matrix space. SLC25A16 is 35%
identical to the yeast mitochondrial carrier protein Leu5. In yeast
strains lacking Leu5, Prohl et al. (2001) detected reduced
mitochondrial, but not cytosolic, CoA levels. Organelles from
Leu5-negative cells were not capable of synthesis of
alpha-isopropylmalate (IPM) because the IPM synthase was trapped in the
mitochondria. Mutant yeast also lacked peroxisomal citrate synthase.
Transformation of mutant yeast cells with a plasmid carrying SLC25A16 at
least partially replaced Leu5 function, suggesting a role for SLC25A16
in mitochondrial function.
*FIELD* RF
1. Prohl, C.; Pelzer, W.; Diekert, K.; Kmita, H.; Bedekovics, T.;
Kispal, G.; Lill, R.: The yeast mitochondrial carrier Leu5p and its
human homologue Graves' disease protein are required for accumulation
of coenzyme A in the matrix. Molec. Cell Biol. 21: 1089-1097, 2001.
2. Rossi, E.; Zarrilli, R.; Zuffardi, O.: Regional assignment of
the gene coding for a human Graves' disease autoantigen to 10q21.3-q22.1. Hum.
Genet. 90: 653-654, 1993.
3. Zarrilli, R.; Oates, E. L.; McBride, O. W.; Lerman, M. I.; Chan,
J. Y.; Santisteban, P.; Ursini, M. V.; Notkins, A. L.; Kohn, L. D.
: Sequence and chromosomal assignment of a novel cDNA identified by
immunoscreening of a thyroid expression library: similarity to a family
of mitochondrial solute carrier proteins. Molec. Endocr. 3: 1498-1508,
1989.
*FIELD* CD
Victor A. McKusick: 4/27/1993
*FIELD* ED
cwells: 11/12/2003
mgross: 5/11/2001
mcapotos: 5/11/2001
mcapotos: 5/10/2001
psherman: 7/29/1999
psherman: 7/23/1998
mark: 6/5/1996
terry: 6/3/1996
mimadm: 9/24/1994
carol: 5/16/1994
carol: 10/26/1993
carol: 4/27/1993