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Protein MGARP (Corneal endothelium-specific protein 1) (CESP-1) (Hypoxia up-regulated mitochondrial movement regulator protein) (Mitochondria-localized glutamic acid-rich protein) (Ovary-specific acidic protein)

 HUMMR_MOUSE             Reviewed;         283 AA.
Q8VI64; Q96EB2; Q9D9Y5;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
05-JUL-2017, entry version 90.
RecName: Full=Protein MGARP;
AltName: Full=Corneal endothelium-specific protein 1;
Short=CESP-1;
AltName: Full=Hypoxia up-regulated mitochondrial movement regulator protein;
AltName: Full=Mitochondria-localized glutamic acid-rich protein;
AltName: Full=Ovary-specific acidic protein;
Name=Mgarp; Synonyms=Cesp1, Hummr, Osap;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary;
PubMed=10919256; DOI=10.1210/endo.141.8.7627;
Hennebold J.D., Tanaka M., Saito J., Hanson B.R., Adashi E.Y.;
"Ovary-selective genes I: the generation and characterization of an
ovary-selective complementary deoxyribonucleic acid library.";
Endocrinology 141:2725-2734(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone marrow;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
TISSUE SPECIFICITY.
PubMed=16565373; DOI=10.1167/iovs.05-0602;
Kinouchi R., Kinouchi T., Hamamoto T., Saito T., Tavares A., Tsuru T.,
Yamagami S.;
"Distribution of CESP-1 protein in the corneal endothelium and other
tissues.";
Invest. Ophthalmol. Vis. Sci. 47:1397-1403(2006).
[5]
FUNCTION IN STEROIDOGENESIS, SUBCELLULAR LOCATION, INDUCTION, AND
TISSUE SPECIFICITY.
PubMed=19325000; DOI=10.1210/en.2008-1584;
Matsumoto T., Minegishi K., Ishimoto H., Tanaka M., Hennebold J.D.,
Teranishi T., Hattori Y., Furuya M., Higuchi T., Asai S., Kim S.H.,
Miyakoshi K., Yoshimura Y.;
"Expression of ovary-specific acidic protein in steroidogenic tissues:
a possible role in steroidogenesis.";
Endocrinology 150:3353-3359(2009).
[6]
FUNCTION IN MITOCHONDRIAL TRANSPORT, INTERACTION WITH RHOT1; RHOT2;
TRAK1 AND TRAK2, TOPOLOGY, INDUCTION, DISRUPTION PHENOTYPE,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19528298; DOI=10.1083/jcb.200811033;
Li Y., Lim S., Hoffman D., Aspenstrom P., Federoff H.J., Rempe D.A.;
"HUMMR, a hypoxia- and HIF-1alpha-inducible protein, alters
mitochondrial distribution and transport.";
J. Cell Biol. 185:1065-1081(2009).
[7]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=21447634; DOI=10.1210/en.2011-0050;
Zhou M., Wang Y., Qi S., Wang J., Zhang S.;
"The expression of a mitochondria-localized glutamic acid-rich protein
(MGARP/OSAP) is under the regulation of the HPG axis.";
Endocrinology 152:2311-2320(2011).
[8]
SUBCELLULAR LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
PubMed=20107910; DOI=10.1007/s11033-010-9948-x;
Qi S., Wang Y., Zhou M., Ge Y., Yan Y., Wang J., Zhang S.S., Zhang S.;
"A mitochondria-localized glutamic acid-rich protein (MGARP/OSAP) is
highly expressed in retina that exhibits a large area of intrinsic
disorder.";
Mol. Biol. Rep. 38:2869-2877(2011).
-!- FUNCTION: Plays a role in the trafficking of mitochondria along
microtubules. Regulates the kinesin-mediated axonal transport of
mitochondria to nerve terminals along microtubules during hypoxia.
Participates in the translocation of TRAK2/GRIF1 from the
cytoplasm to the mitochondrion. Also plays a role in
steroidogenesis through maintenance of mitochondrial abundance and
morphology. {ECO:0000269|PubMed:19325000,
ECO:0000269|PubMed:19528298}.
-!- SUBUNIT: Interacts with RHOT1/Miro-1, RHOT2/Miro-2, TRAK1/OIP106
and TRAK2/GRIF1. {ECO:0000269|PubMed:19528298}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19325000,
ECO:0000269|PubMed:19528298, ECO:0000269|PubMed:20107910,
ECO:0000269|PubMed:21447634}. Mitochondrion outer membrane
{ECO:0000269|PubMed:19325000, ECO:0000269|PubMed:19528298,
ECO:0000269|PubMed:20107910, ECO:0000269|PubMed:21447634}; Single-
pass type IV membrane protein {ECO:0000269|PubMed:19325000,
ECO:0000269|PubMed:19528298, ECO:0000269|PubMed:20107910,
ECO:0000269|PubMed:21447634}; Cytoplasmic side
{ECO:0000269|PubMed:19325000, ECO:0000269|PubMed:19528298,
ECO:0000269|PubMed:20107910, ECO:0000269|PubMed:21447634}.
Note=Colocalizes with RHOT1, RHOT2, TRAK1 and TRAK2 at the
mitochondrion (PubMed:19528298).
-!- TISSUE SPECIFICITY: Expressed in the ovary, testis, brain, adrenal
glands and the compartments of the visual nervous system.
Expressed in corneal endothelium (CE) (at protein level).
Expressed in steroidogenic tissues with the highest level of
expression observed in the adrenal gland. Weakly expressed in
placenta. Weakly expressed in astrocytes and neurons under
normoxia. Strongly expressed in astrocytes and neurons under
hypoxia. Expressed in each layer of the retina, with particularly
higher staining in the inner segment of the photoreceptor (IS),
the outer plexiform layer (OPL) and the ganglion cell layer (GCL).
{ECO:0000269|PubMed:16565373, ECO:0000269|PubMed:19325000,
ECO:0000269|PubMed:19528298, ECO:0000269|PubMed:20107910,
ECO:0000269|PubMed:21447634}.
-!- INDUCTION: Up-regulated by chorionic gonadotropin in ovary. Up-
regulated by hypoxia in a HIF-1A-dependent manner in neurons and
astrocytes. Up-regulated during gonad development after birth,
probably under the regulation of hormones derived from the
hypothalamic-pituitary-gonadal (HPG) axis.
{ECO:0000269|PubMed:19325000, ECO:0000269|PubMed:19528298,
ECO:0000269|PubMed:20107910}.
-!- DISRUPTION PHENOTYPE: Reduction of mitochondrial motion in the
anterograde direction and increase of mitochondrial motion in the
retrograde direction in response to hypoxia. The number of motile
mitochondria is not altered. {ECO:0000269|PubMed:19528298}.
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EMBL; AF228502; AAL55654.1; -; mRNA.
EMBL; AK006339; BAB24535.1; -; mRNA.
EMBL; AK151401; BAE30369.1; -; mRNA.
EMBL; BC012511; AAH12511.1; -; mRNA.
EMBL; BC049556; AAH49556.1; -; mRNA.
CCDS; CCDS17338.1; -.
RefSeq; NP_080634.2; NM_026358.3.
UniGene; Mm.273339; -.
ProteinModelPortal; Q8VI64; -.
PhosphoSitePlus; Q8VI64; -.
MaxQB; Q8VI64; -.
PaxDb; Q8VI64; -.
PRIDE; Q8VI64; -.
Ensembl; ENSMUST00000038154; ENSMUSP00000040703; ENSMUSG00000037161.
GeneID; 67749; -.
KEGG; mmu:67749; -.
UCSC; uc008pdx.2; mouse.
CTD; 84709; -.
MGI; MGI:1914999; Mgarp.
eggNOG; ENOG410IWK1; Eukaryota.
eggNOG; ENOG410Y7BU; LUCA.
GeneTree; ENSGT00440000037338; -.
HOGENOM; HOG000111473; -.
InParanoid; Q8VI64; -.
PhylomeDB; Q8VI64; -.
TreeFam; TF336324; -.
PRO; PR:Q8VI64; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000037161; -.
CleanEx; MM_4930583H14RIK; -.
ExpressionAtlas; Q8VI64; baseline and differential.
Genevisible; Q8VI64; MM.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0008089; P:anterograde axonal transport; IMP:UniProtKB.
GO; GO:0019896; P:axonal transport of mitochondrion; IMP:UniProtKB.
GO; GO:0097211; P:cellular response to gonadotropin-releasing hormone; IDA:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
GO; GO:0071383; P:cellular response to steroid hormone stimulus; IMP:UniProtKB.
GO; GO:0010822; P:positive regulation of mitochondrion organization; IMP:UniProtKB.
GO; GO:0006626; P:protein targeting to mitochondrion; IDA:UniProtKB.
GO; GO:0008090; P:retrograde axonal transport; IMP:UniProtKB.
InterPro; IPR026093; MGARP.
InterPro; IPR032773; MGARP_N.
PANTHER; PTHR22910; PTHR22910; 1.
Pfam; PF14962; AIF-MLS; 1.
1: Evidence at protein level;
Complete proteome; Membrane; Mitochondrion;
Mitochondrion outer membrane; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 283 Protein MGARP.
/FTId=PRO_0000318765.
TOPO_DOM 1 41 Cytoplasmic. {ECO:0000255}.
TRANSMEM 42 64 Helical; Anchor for type IV membrane
protein.
TOPO_DOM 65 283 Mitochondrial intermembrane.
{ECO:0000255}.
COMPBIAS 76 277 Glu-rich.
CONFLICT 4 4 R -> S (in Ref. 2; BAB24535).
{ECO:0000305}.
SEQUENCE 283 AA; 29925 MW; AFF16FC5E70536CF CRC64;
MYLRRAVSKT LALPRRAPPG PAPLGKDASL RRMSSRKFPG TSGSNMIYYL VVGVTVSAGG
YYTYKALTSK QVRRTEHVAE PKEQTKAELQ PLPGEKEEHV AEAEQVCSEP GDTAVTEAES
VDAEEVPEAA VVLPEESQAS APSEVPAEAA VVEASLSSSE PELKITEASL VETTESVPES
TQEVESAAPD QDDVCNEGAD TSQEGADTSQ EGADTSQEGA DTTKEEADNS KEAEGTTTED
PRSISEESAE LEESPPLGSE PPAQPESQEE ETQVTEETAS PQG


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