CS012_HUMAN
ID CS012_HUMAN Reviewed; 152 AA.
AC Q9NSK7; B3KQ16; Q0D2Q0; Q6P4C5; Q9BSL7;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Protein C19orf12;
GN Name=C19orf12;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-144 (ISOFORM 4).
RC TISSUE=Stomach, and Teratocarcinoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 72-152 (ISOFORMS 1/4).
RC TISSUE=Brain, Lymph, and Ovary;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 34-141 (ISOFORMS 1/2).
RC TISSUE=Melanoma;
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 [5]
RP INVOLVEMENT IN NBIA4.
RX PubMed=23521069; DOI=10.1111/cge.12137;
RA Schottmann G., Stenzel W., Lutzkendorf S., Schuelke M., Knierim E.;
RT "A novel frameshift mutation of C19ORF12 causes NBIA4 with cerebellar
RT atrophy and manifests with severe peripheral motor axonal neuropathy.";
RL Clin. Genet. 85:290-292(2014).
RN [6]
RP VARIANTS NBIA4 MET-11; ARG-53; GLU-65 AND ARG-69, VARIANTS GLU-142 AND
RP THR-142, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=21981780; DOI=10.1016/j.ajhg.2011.09.007;
RA Hartig M.B., Iuso A., Haack T., Kmiec T., Jurkiewicz E., Heim K.,
RA Roeber S., Tarabin V., Dusi S., Krajewska-Walasek M., Jozwiak S.,
RA Hempel M., Winkelmann J., Elstner M., Oexle K., Klopstock T.,
RA Mueller-Felber W., Gasser T., Trenkwalder C., Tiranti V., Kretzschmar H.,
RA Schmitz G., Strom T.M., Meitinger T., Prokisch H.;
RT "Absence of an orphan mitochondrial protein, c19orf12, causes a distinct
RT clinical subtype of neurodegeneration with brain iron accumulation.";
RL Am. J. Hum. Genet. 89:543-550(2011).
RN [7]
RP VARIANTS NBIA4 MET-11 AND GLY-66 DEL.
RX PubMed=22584950; DOI=10.1007/s00415-012-6521-7;
RA Deschauer M., Gaul C., Behrmann C., Prokisch H., Zierz S., Haack T.B.;
RT "C19orf12 mutations in neurodegeneration with brain iron accumulation
RT mimicking juvenile amyotrophic lateral sclerosis.";
RL J. Neurol. 259:2434-2439(2012).
RN [8]
RP VARIANT NBIA4 GLN-121.
RX PubMed=22508347; DOI=10.1002/mds.24980;
RA Horvath R., Holinski-Feder E., Neeve V.C., Pyle A., Griffin H., Ashok D.,
RA Foley C., Hudson G., Rautenstrauss B., Nurnberg G., Nurnberg P.,
RA Kortler J., Neitzel B., Bassmann I., Rahman T., Keavney B., Loughlin J.,
RA Hambleton S., Schoser B., Lochmuller H., Santibanez-Koref M.,
RA Chinnery P.F.;
RT "A new phenotype of brain iron accumulation with dystonia, optic atrophy,
RT and peripheral neuropathy.";
RL Mov. Disord. 27:789-793(2012).
RN [9]
RP VARIANTS NBIA4 SER-58 AND PRO-96.
RX PubMed=22704260; DOI=10.1016/j.spen.2012.03.006;
RA Panteghini C., Zorzi G., Venco P., Dusi S., Reale C., Brunetti D.,
RA Chiapparini L., Zibordi F., Siegel B., Siegel B., Garavaglia B.,
RA Simonati A., Bertini E., Nardocci N., Tiranti V.;
RT "C19orf12 and FA2H mutations are rare in Italian patients with
RT neurodegeneration with brain iron accumulation.";
RL Semin. Pediatr. Neurol. 19:75-81(2012).
RN [10]
RP VARIANT NBIA4 MET-11.
RX PubMed=23278385; DOI=10.1111/cge.12079;
RA Dogu O., Krebs C.E., Kaleagasi H., Demirtas Z., Oksuz N., Walker R.H.,
RA Paisan-Ruiz C.;
RT "Rapid disease progression in adult-onset mitochondrial membrane protein-
RT associated neurodegeneration.";
RL Clin. Genet. 84:350-355(2013).
RN [11]
RP VARIANTS NBIA4 PHE-39; PRO-48; ARG-53; LEU-60; GLU-65; VAL-65; ARG-69;
RP LEU-83; SER-98 AND PRO-134, AND VARIANTS GLU-142; THR-142 AND ARG-149.
RX PubMed=23269600; DOI=10.1212/wnl.0b013e31827e07be;
RA Hogarth P., Gregory A., Kruer M.C., Sanford L., Wagoner W., Natowicz M.R.,
RA Egel R.T., Subramony S.H., Goldman J.G., Berry-Kravis E., Foulds N.C.,
RA Hammans S.R., Desguerre I., Rodriguez D., Wilson C., Diedrich A., Green S.,
RA Tran H., Reese L., Woltjer R.L., Hayflick S.J.;
RT "New NBIA subtype: genetic, clinical, pathologic, and radiographic features
RT of MPAN.";
RL Neurology 80:268-275(2013).
RN [12]
RP VARIANT SPG43 PRO-63, VARIANTS NBIA4 PRO-63 AND GLY-66 DEL, SUBCELLULAR
RP LOCATION, CHARACTERIZATION OF VARIANTS SPG43 PRO-63, AND CHARACTERIZATION
RP OF VARIANTS NBIA4 PRO-63; GLY-66 DEL AND ARG-69.
RX PubMed=23857908; DOI=10.1002/humu.22378;
RA Landoure G., Zhu P.P., Lourenco C.M., Johnson J.O., Toro C., Bricceno K.V.,
RA Rinaldi C., Meilleur K.G., Sangare M., Diallo O., Pierson T.M., Ishiura H.,
RA Tsuji S., Hein N., Fink J.K., Stoll M., Nicholson G., Gonzalez M.A.,
RA Speziani F., Durr A., Stevanin G., Biesecker L.G., Accardi J., Landis D.M.,
RA Gahl W.A., Traynor B.J., Marques W. Jr., Zuchner S., Blackstone C.,
RA Fischbeck K.H., Burnett B.G.;
RT "Hereditary spastic paraplegia type 43 (SPG43) is caused by mutation in
RT C19orf12.";
RL Hum. Mutat. 34:1357-1360(2013).
RN [13]
RP CHARACTERIZATION OF VARIANTS NBIA4 SER-58 AND PRO-96, AND SUBCELLULAR
RP LOCATION.
RX PubMed=26136767; DOI=10.3389/fgene.2015.00185;
RA Venco P., Bonora M., Giorgi C., Papaleo E., Iuso A., Prokisch H.,
RA Pinton P., Tiranti V.;
RT "Mutations of C19orf12, coding for a transmembrane glycine zipper
RT containing mitochondrial protein, cause mis-localization of the protein,
RT inability to respond to oxidative stress and increased mitochondrial
RT Ca(2)(+).";
RL Front. Genet. 6:185-185(2015).
RN [14]
RP VARIANTS NBIA4 MET-11 AND ARG-69.
RX PubMed=25592411; DOI=10.1016/j.jns.2014.12.036;
RA Tschentscher A., Dekomien G., Ross S., Cremer K., Kukuk G.M., Epplen J.T.,
RA Hoffjan S.;
RT "Analysis of the C19orf12 and WDR45 genes in patients with
RT neurodegeneration with brain iron accumulation.";
RL J. Neurol. Sci. 349:105-109(2015).
RN [15]
RP VARIANT NBIA4 LEU-83.
RX PubMed=26187298; DOI=10.1016/j.jns.2015.07.009;
RA Kleffner I., Wessling C., Gess B., Korsukewitz C., Allkemper T.,
RA Schirmacher A., Young P., Senderek J., Husstedt I.W.;
RT "Behr syndrome with homozygous C19ORF12 mutation.";
RL J. Neurol. Sci. 357:115-118(2015).
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21981780,
CC ECO:0000269|PubMed:22508347, ECO:0000269|PubMed:26136767}.
CC Mitochondrion membrane {ECO:0000269|PubMed:21981780,
CC ECO:0000269|PubMed:26136767}; Single-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:22508347}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:26136767}. Note=In response to
CC oxidative stress, relocates to the cytosol forming aggregates that
CC partially co-localize with mitochondria. {ECO:0000269|PubMed:26136767}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=4;
CC IsoId=Q9NSK7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NSK7-2; Sequence=VSP_027227;
CC Name=3;
CC IsoId=Q9NSK7-3; Sequence=VSP_037995, VSP_027228;
CC Name=1;
CC IsoId=Q9NSK7-4; Sequence=VSP_037995;
CC -!- INDUCTION: Up-regulated during adipocyte differentiation in an in vitro
CC preadipocyte differentiation model. {ECO:0000269|PubMed:21981780}.
CC -!- DISEASE: Neurodegeneration with brain iron accumulation 4 (NBIA4)
CC [MIM:614298]: A neurodegenerative disorder associated with iron
CC accumulation in the brain, primarily in the basal ganglia. NBIA4
CC results in speech difficulty, extrapyramidal signs, oromandibular and
CC generalized dystonia, and parkinsonism. Most patients have progressive
CC involvement of the corticospinal tract, with spasticity, hyperreflexia,
CC and extensor plantar responses. {ECO:0000269|PubMed:21981780,
CC ECO:0000269|PubMed:22508347, ECO:0000269|PubMed:22584950,
CC ECO:0000269|PubMed:22704260, ECO:0000269|PubMed:23269600,
CC ECO:0000269|PubMed:23278385, ECO:0000269|PubMed:23521069,
CC ECO:0000269|PubMed:23857908, ECO:0000269|PubMed:25592411,
CC ECO:0000269|PubMed:26136767, ECO:0000269|PubMed:26187298}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Spastic paraplegia 43, autosomal recessive (SPG43)
CC [MIM:615043]: A form of spastic paraplegia, a neurodegenerative
CC disorder characterized by a slow, gradual, progressive weakness and
CC spasticity of the lower limbs. Rate of progression and the severity of
CC symptoms are quite variable. Initial symptoms may include difficulty
CC with balance, weakness and stiffness in the legs, muscle spasms, and
CC dragging the toes when walking. In some forms of the disorder, bladder
CC symptoms (such as incontinence) may appear, or the weakness and
CC stiffness may spread to other parts of the body. SP43 is characterized
CC by childhood onset of progressive spasticity affecting the lower and
CC upper limbs. {ECO:0000269|PubMed:23857908}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the C19orf12 family. {ECO:0000305}.
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DR EMBL; AK057185; BAG51878.1; -; mRNA.
DR EMBL; DA708831; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC010513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004957; AAH04957.1; -; mRNA.
DR EMBL; BC009946; AAH09946.1; -; mRNA.
DR EMBL; BC063518; AAH63518.1; -; mRNA.
DR EMBL; BC017211; AAH17211.2; -; mRNA.
DR EMBL; AL162066; CAB82403.1; -; mRNA.
DR CCDS; CCDS12418.2; -. [Q9NSK7-4]
DR CCDS; CCDS42542.1; -. [Q9NSK7-4]
DR CCDS; CCDS59373.1; -. [Q9NSK7-3]
DR CCDS; CCDS74325.1; -. [Q9NSK7-2]
DR PIR; T47169; T47169.
DR RefSeq; NP_001026896.2; NM_001031726.3. [Q9NSK7-1]
DR RefSeq; NP_001242975.1; NM_001256046.1. [Q9NSK7-3]
DR RefSeq; NP_001242976.1; NM_001256047.1. [Q9NSK7-4]
DR RefSeq; NP_001269858.1; NM_001282929.1. [Q9NSK7-2]
DR RefSeq; NP_001269859.1; NM_001282930.1. [Q9NSK7-2]
DR RefSeq; NP_001269860.1; NM_001282931.1. [Q9NSK7-2]
DR RefSeq; NP_113636.2; NM_031448.4. [Q9NSK7-4]
DR AlphaFoldDB; Q9NSK7; -.
DR BioGRID; 123700; 2.
DR IntAct; Q9NSK7; 2.
DR STRING; 9606.ENSP00000376103; -.
DR iPTMnet; Q9NSK7; -.
DR PhosphoSitePlus; Q9NSK7; -.
DR BioMuta; C19orf12; -.
DR DMDM; 374095505; -.
DR EPD; Q9NSK7; -.
DR jPOST; Q9NSK7; -.
DR MassIVE; Q9NSK7; -.
DR MaxQB; Q9NSK7; -.
DR PaxDb; Q9NSK7; -.
DR PeptideAtlas; Q9NSK7; -.
DR PRIDE; Q9NSK7; -.
DR ProteomicsDB; 82566; -. [Q9NSK7-1]
DR ProteomicsDB; 82567; -. [Q9NSK7-2]
DR ProteomicsDB; 82568; -. [Q9NSK7-3]
DR ProteomicsDB; 82569; -. [Q9NSK7-4]
DR Antibodypedia; 47936; 42 antibodies from 15 providers.
DR DNASU; 83636; -.
DR Ensembl; ENST00000323670.14; ENSP00000313332.9; ENSG00000131943.20. [Q9NSK7-4]
DR Ensembl; ENST00000392275.1; ENSP00000507573.1; ENSG00000131943.20. [Q9NSK7-2]
DR Ensembl; ENST00000392276.1; ENSP00000376102.1; ENSG00000131943.20. [Q9NSK7-2]
DR Ensembl; ENST00000592153.5; ENSP00000467117.1; ENSG00000131943.20. [Q9NSK7-3]
DR Ensembl; ENST00000623113.3; ENSP00000485413.2; ENSG00000131943.20. [Q9NSK7-4]
DR GeneID; 83636; -.
DR KEGG; hsa:83636; -.
DR MANE-Select; ENST00000323670.14; ENSP00000313332.9; NM_031448.6; NP_113636.2. [Q9NSK7-4]
DR UCSC; uc002nsj.4; human. [Q9NSK7-1]
DR CTD; 83636; -.
DR DisGeNET; 83636; -.
DR GeneCards; C19orf12; -.
DR GeneReviews; C19orf12; -.
DR HGNC; HGNC:25443; C19orf12.
DR HPA; ENSG00000131943; Tissue enhanced (adipose tissue, tongue).
DR MalaCards; C19orf12; -.
DR MIM; 614297; gene.
DR MIM; 614298; phenotype.
DR MIM; 615043; phenotype.
DR neXtProt; NX_Q9NSK7; -.
DR OpenTargets; ENSG00000131943; -.
DR Orphanet; 320370; Autosomal recessive spastic paraplegia type 43.
DR Orphanet; 289560; Mitochondrial membrane protein-associated neurodegeneration.
DR PharmGKB; PA134981038; -.
DR VEuPathDB; HostDB:ENSG00000131943; -.
DR eggNOG; ENOG502RZQC; Eukaryota.
DR GeneTree; ENSGT00390000009077; -.
DR HOGENOM; CLU_2460310_0_0_1; -.
DR InParanoid; Q9NSK7; -.
DR OrthoDB; 1474873at2759; -.
DR PhylomeDB; Q9NSK7; -.
DR TreeFam; TF323308; -.
DR PathwayCommons; Q9NSK7; -.
DR SignaLink; Q9NSK7; -.
DR BioGRID-ORCS; 83636; 23 hits in 1067 CRISPR screens.
DR ChiTaRS; C19orf12; human.
DR GenomeRNAi; 83636; -.
DR Pharos; Q9NSK7; Tbio.
DR PRO; PR:Q9NSK7; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NSK7; protein.
DR Bgee; ENSG00000131943; Expressed in endothelial cell and 184 other tissues.
DR ExpressionAtlas; Q9NSK7; baseline and differential.
DR Genevisible; Q9NSK7; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
DR GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR InterPro; IPR033369; C19orf12.
DR PANTHER; PTHR31493; PTHR31493; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Disease variant; Endoplasmic reticulum;
KW Hereditary spastic paraplegia; Membrane; Mitochondrion; Neurodegeneration;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..152
FT /note="Protein C19orf12"
FT /id="PRO_0000296662"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..75
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027227"
FT VAR_SEQ 1..11
FT /note="Missing (in isoform 1 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_037995"
FT VAR_SEQ 109..152
FT /note="HLEWTDAVQLTALVMGSEALQQQLLAMLVNYVTKELRAEIQYDD -> PCSS
FT SCWPCW (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027228"
FT VARIANT 11
FT /note="T -> M (in NBIA4; dbSNP:rs397514477)"
FT /evidence="ECO:0000269|PubMed:21981780,
FT ECO:0000269|PubMed:22584950, ECO:0000269|PubMed:23278385,
FT ECO:0000269|PubMed:25592411"
FT /id="VAR_066617"
FT VARIANT 39
FT /note="S -> F (in NBIA4; dbSNP:rs1204865094)"
FT /evidence="ECO:0000269|PubMed:23269600"
FT /id="VAR_069756"
FT VARIANT 48
FT /note="A -> P (in NBIA4)"
FT /evidence="ECO:0000269|PubMed:23269600"
FT /id="VAR_069757"
FT VARIANT 53
FT /note="G -> R (in NBIA4; dbSNP:rs200133991)"
FT /evidence="ECO:0000269|PubMed:21981780,
FT ECO:0000269|PubMed:23269600"
FT /id="VAR_066618"
FT VARIANT 58
FT /note="G -> S (in NBIA4; predominantly cytosolic
FT distribution with a localization also seen in the
FT mitochondrial matrix; no cytosolic redistribution seen in
FT response to oxidative stress; patient fibroblasts
FT accumulate high levels of mitochondrial calcium and are
FT more prone to oxidative stress-induced apoptosis;
FT dbSNP:rs1358503478)"
FT /evidence="ECO:0000269|PubMed:22704260,
FT ECO:0000269|PubMed:26136767"
FT /id="VAR_076803"
FT VARIANT 60
FT /note="P -> L (in NBIA4; dbSNP:rs1424999393)"
FT /evidence="ECO:0000269|PubMed:23269600"
FT /id="VAR_069758"
FT VARIANT 63
FT /note="A -> P (in NBIA4 and SPG43; impairs subcellular
FT localization to the endoplasmic reticulum or mitochondrion;
FT dbSNP:rs376103979)"
FT /evidence="ECO:0000269|PubMed:23857908"
FT /id="VAR_070668"
FT VARIANT 65
FT /note="G -> E (in NBIA4; dbSNP:rs752450983)"
FT /evidence="ECO:0000269|PubMed:21981780,
FT ECO:0000269|PubMed:23269600"
FT /id="VAR_066619"
FT VARIANT 65
FT /note="G -> V (in NBIA4; dbSNP:rs752450983)"
FT /evidence="ECO:0000269|PubMed:23269600"
FT /id="VAR_069759"
FT VARIANT 66
FT /note="Missing (in NBIA4; impairs subcellular localization
FT to the endoplasmic reticulum or mitochondrion)"
FT /evidence="ECO:0000269|PubMed:22584950,
FT ECO:0000269|PubMed:23857908"
FT /id="VAR_070669"
FT VARIANT 69
FT /note="G -> R (in NBIA4; impairs subcellular localization
FT to the endoplasmic reticulum or mitochondrion;
FT dbSNP:rs515726205)"
FT /evidence="ECO:0000269|PubMed:21981780,
FT ECO:0000269|PubMed:23269600, ECO:0000269|PubMed:23857908,
FT ECO:0000269|PubMed:25592411"
FT /id="VAR_066620"
FT VARIANT 83
FT /note="P -> L (in NBIA4; dbSNP:rs201987973)"
FT /evidence="ECO:0000269|PubMed:23269600,
FT ECO:0000269|PubMed:26187298"
FT /id="VAR_069760"
FT VARIANT 96
FT /note="Q -> P (in NBIA4; no effect on its subcellular
FT localization; no cytosolic redistribution seen in response
FT to oxidative stress)"
FT /evidence="ECO:0000269|PubMed:22704260,
FT ECO:0000269|PubMed:26136767"
FT /id="VAR_076804"
FT VARIANT 98
FT /note="R -> S (in NBIA4; dbSNP:rs1384930997)"
FT /evidence="ECO:0000269|PubMed:23269600"
FT /id="VAR_069761"
FT VARIANT 121
FT /note="L -> Q (in NBIA4)"
FT /evidence="ECO:0000269|PubMed:22508347"
FT /id="VAR_069762"
FT VARIANT 134
FT /note="A -> P (in NBIA4; unknown pathological significance;
FT dbSNP:rs1264612218)"
FT /evidence="ECO:0000269|PubMed:23269600"
FT /id="VAR_069763"
FT VARIANT 142
FT /note="K -> E (found in families with neurodegeneration
FT with brain iron accumulation; uncertain pathological
FT significance; dbSNP:rs146170087)"
FT /evidence="ECO:0000269|PubMed:21981780,
FT ECO:0000269|PubMed:23269600"
FT /id="VAR_066621"
FT VARIANT 142
FT /note="K -> T (in dbSNP:rs79915936)"
FT /evidence="ECO:0000269|PubMed:21981780,
FT ECO:0000269|PubMed:23269600"
FT /id="VAR_066622"
FT VARIANT 149
FT /note="Q -> R (in dbSNP:rs73023451)"
FT /evidence="ECO:0000269|PubMed:23269600"
FT /id="VAR_069764"
SQ SEQUENCE 152 AA; 16286 MW; F8C1300487F99BD5 CRC64;
MERLKSHKPA TMTIMVEDIM KLLCSLSGER KMKAAVKHSG KGALVTGAMA FVGGLVGGPP
GLAVGGAVGG LLGAWMTSGQ FKPVPQILME LPPAEQQRLF NEAAAIIRHL EWTDAVQLTA
LVMGSEALQQ QLLAMLVNYV TKELRAEIQY DD
