HUMMR_HUMAN
ID HUMMR_HUMAN Reviewed; 240 AA.
AC Q8TDB4; Q9BZC3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Protein MGARP;
DE AltName: Full=Corneal endothelium-specific protein 1;
DE Short=CESP-1;
DE AltName: Full=Hypoxia up-regulated mitochondrial movement regulator protein;
DE AltName: Full=Mitochondria-localized glutamic acid-rich protein;
DE AltName: Full=Ovary-specific acidic protein;
GN Name=MGARP; Synonyms=C4orf49, CESP1, HUMMR, OSAP; ORFNames=GS3582;
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 TISSUE SPECIFICITY.
RC TISSUE=Corneal endothelium;
RX PubMed=12036975;
RA Sakai R., Kinouchi T., Kawamoto S., Dana M.R., Hamamoto T., Tsuru T.,
RA Okubo K., Yamagami S.;
RT "Construction of human corneal endothelial cDNA library and identification
RT of novel active genes.";
RL Invest. Ophthalmol. Vis. Sci. 43:1749-1756(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Ovary;
RX PubMed=12770732; DOI=10.1016/s0303-7207(03)00064-9;
RA Tanaka M., Hennebold J.D., Miyakoshi K., Teranishi T., Ueno K.,
RA Adashi E.Y.;
RT "The generation and characterization of an ovary-selective cDNA library.";
RL Mol. Cell. Endocrinol. 202:67-69(2003).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16565373; DOI=10.1167/iovs.05-0602;
RA Kinouchi R., Kinouchi T., Hamamoto T., Saito T., Tavares A., Tsuru T.,
RA Yamagami S.;
RT "Distribution of CESP-1 protein in the corneal endothelium and other
RT tissues.";
RL Invest. Ophthalmol. Vis. Sci. 47:1397-1403(2006).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=19325000; DOI=10.1210/en.2008-1584;
RA Matsumoto T., Minegishi K., Ishimoto H., Tanaka M., Hennebold J.D.,
RA Teranishi T., Hattori Y., Furuya M., Higuchi T., Asai S., Kim S.H.,
RA Miyakoshi K., Yoshimura Y.;
RT "Expression of ovary-specific acidic protein in steroidogenic tissues: a
RT possible role in steroidogenesis.";
RL Endocrinology 150:3353-3359(2009).
RN [7]
RP INTERACTION WITH RHOT2, AND TISSUE SPECIFICITY.
RX PubMed=19528298; DOI=10.1083/jcb.200811033;
RA Li Y., Lim S., Hoffman D., Aspenstrom P., Federoff H.J., Rempe D.A.;
RT "HUMMR, a hypoxia- and HIF-1alpha-inducible protein, alters mitochondrial
RT distribution and transport.";
RL J. Cell Biol. 185:1065-1081(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=21447634; DOI=10.1210/en.2011-0050;
RA Zhou M., Wang Y., Qi S., Wang J., Zhang S.;
RT "The expression of a mitochondria-localized glutamic acid-rich protein
RT (MGARP/OSAP) is under the regulation of the HPG axis.";
RL Endocrinology 152:2311-2320(2011).
CC -!- FUNCTION: Plays a role in the trafficking of mitochondria along
CC microtubules. Regulates the kinesin-mediated axonal transport of
CC mitochondria to nerve terminals along microtubules during hypoxia.
CC Participates in the translocation of TRAK2/GRIF1 from the cytoplasm to
CC the mitochondrion. Also plays a role in steroidogenesis through
CC maintenance of mitochondrial abundance and morphology (By similarity).
CC Plays an inhibitory role during neocortex development by regulating
CC mitochondrial morphology, distribution and motility in neocortical
CC neurons (By similarity). {ECO:0000250|UniProtKB:Q8VI64}.
CC -!- SUBUNIT: Interacts with RHOT1/Miro-1, TRAK1/OIP106 and TRAK2/GRIF1 (By
CC similarity). Interacts with RHOT2/Miro-2.
CC {ECO:0000250|UniProtKB:Q8VI64, ECO:0000269|PubMed:19528298}.
CC -!- INTERACTION:
CC Q8TDB4; P01023: A2M; NbExp=3; IntAct=EBI-4397720, EBI-640741;
CC Q8TDB4; A0A0S2Z5Q7: ALS2; NbExp=3; IntAct=EBI-4397720, EBI-25928834;
CC Q8TDB4; Q92870-2: APBB2; NbExp=3; IntAct=EBI-4397720, EBI-21535880;
CC Q8TDB4; P05067: APP; NbExp=3; IntAct=EBI-4397720, EBI-77613;
CC Q8TDB4; P05067-2: APP; NbExp=3; IntAct=EBI-4397720, EBI-17264467;
CC Q8TDB4; P54253: ATXN1; NbExp=6; IntAct=EBI-4397720, EBI-930964;
CC Q8TDB4; P50570-2: DNM2; NbExp=3; IntAct=EBI-4397720, EBI-10968534;
CC Q8TDB4; Q8TB36: GDAP1; NbExp=3; IntAct=EBI-4397720, EBI-11110431;
CC Q8TDB4; P42858: HTT; NbExp=21; IntAct=EBI-4397720, EBI-466029;
CC Q8TDB4; P51608: MECP2; NbExp=3; IntAct=EBI-4397720, EBI-1189067;
CC Q8TDB4; Q96CV9: OPTN; NbExp=3; IntAct=EBI-4397720, EBI-748974;
CC Q8TDB4; D3DTS7: PMP22; NbExp=3; IntAct=EBI-4397720, EBI-25882629;
CC Q8TDB4; O60260-5: PRKN; NbExp=6; IntAct=EBI-4397720, EBI-21251460;
CC Q8TDB4; P49768-2: PSEN1; NbExp=6; IntAct=EBI-4397720, EBI-11047108;
CC Q8TDB4; P49810: PSEN2; NbExp=3; IntAct=EBI-4397720, EBI-2010251;
CC Q8TDB4; Q16637: SMN2; NbExp=3; IntAct=EBI-4397720, EBI-395421;
CC Q8TDB4; P37840: SNCA; NbExp=3; IntAct=EBI-4397720, EBI-985879;
CC Q8TDB4; P00441: SOD1; NbExp=3; IntAct=EBI-4397720, EBI-990792;
CC Q8TDB4; Q13148: TARDBP; NbExp=6; IntAct=EBI-4397720, EBI-372899;
CC Q8TDB4; O14656-2: TOR1A; NbExp=3; IntAct=EBI-4397720, EBI-25847109;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16565373,
CC ECO:0000269|PubMed:21447634}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q8VI64}; Single-pass type IV membrane protein
CC {ECO:0000250|UniProtKB:Q8VI64}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q8VI64}. Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q8VI64}; Single-pass type IV membrane protein
CC {ECO:0000250|UniProtKB:Q8VI64}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q8VI64}. Note=Colocalizes with RHOT1, RHOT2,
CC TRAK1 and TRAK2 at the mitochondrion. {ECO:0000250|UniProtKB:Q8VI64}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain, adrenal gland and corneal
CC endothelium (CE). Expressed in steroid-producing cells of the ovary and
CC testis (at protein level). Expressed in steroid-producing cells of the
CC ovary and testis. Weakly expressed in placenta. Expressed in corneal
CC endothelial cells. {ECO:0000269|PubMed:12036975,
CC ECO:0000269|PubMed:12770732, ECO:0000269|PubMed:16565373,
CC ECO:0000269|PubMed:19325000, ECO:0000269|PubMed:19528298}.
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DR EMBL; AF484960; AAM09685.1; -; mRNA.
DR EMBL; AF329088; AAG59896.1; -; mRNA.
DR EMBL; CH471056; EAX05122.1; -; Genomic_DNA.
DR EMBL; BC104173; AAI04174.1; -; mRNA.
DR EMBL; BC104174; AAI04175.1; -; mRNA.
DR CCDS; CCDS43269.1; -.
DR RefSeq; NP_116012.2; NM_032623.3.
DR AlphaFoldDB; Q8TDB4; -.
DR BioGRID; 124220; 257.
DR IntAct; Q8TDB4; 23.
DR MINT; Q8TDB4; -.
DR STRING; 9606.ENSP00000381928; -.
DR iPTMnet; Q8TDB4; -.
DR PhosphoSitePlus; Q8TDB4; -.
DR BioMuta; MGARP; -.
DR DMDM; 74715889; -.
DR jPOST; Q8TDB4; -.
DR MassIVE; Q8TDB4; -.
DR PaxDb; Q8TDB4; -.
DR PeptideAtlas; Q8TDB4; -.
DR PRIDE; Q8TDB4; -.
DR ProteomicsDB; 74255; -.
DR Antibodypedia; 7361; 123 antibodies from 19 providers.
DR DNASU; 84709; -.
DR Ensembl; ENST00000398955.2; ENSP00000381928.1; ENSG00000137463.5.
DR GeneID; 84709; -.
DR KEGG; hsa:84709; -.
DR MANE-Select; ENST00000398955.2; ENSP00000381928.1; NM_032623.4; NP_116012.2.
DR UCSC; uc003ihr.1; human.
DR CTD; 84709; -.
DR DisGeNET; 84709; -.
DR GeneCards; MGARP; -.
DR HGNC; HGNC:29969; MGARP.
DR HPA; ENSG00000137463; Group enriched (adrenal gland, retina).
DR MIM; 619684; gene.
DR neXtProt; NX_Q8TDB4; -.
DR OpenTargets; ENSG00000137463; -.
DR PharmGKB; PA164717327; -.
DR VEuPathDB; HostDB:ENSG00000137463; -.
DR eggNOG; ENOG502S6ZU; Eukaryota.
DR GeneTree; ENSGT00440000037338; -.
DR HOGENOM; CLU_088276_0_0_1; -.
DR InParanoid; Q8TDB4; -.
DR OMA; YTYRTVT; -.
DR OrthoDB; 1441982at2759; -.
DR PhylomeDB; Q8TDB4; -.
DR TreeFam; TF336324; -.
DR PathwayCommons; Q8TDB4; -.
DR SignaLink; Q8TDB4; -.
DR BioGRID-ORCS; 84709; 12 hits in 1073 CRISPR screens.
DR GenomeRNAi; 84709; -.
DR Pharos; Q8TDB4; Tbio.
DR PRO; PR:Q8TDB4; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8TDB4; protein.
DR Bgee; ENSG00000137463; Expressed in adrenal tissue and 107 other tissues.
DR Genevisible; Q8TDB4; HS.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR GO; GO:0061564; P:axon development; ISS:UniProtKB.
DR GO; GO:0019896; P:axonal transport of mitochondrion; ISS:UniProtKB.
DR GO; GO:0097211; P:cellular response to gonadotropin-releasing hormone; ISS:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
DR GO; GO:0071383; P:cellular response to steroid hormone stimulus; ISS:UniProtKB.
DR GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB.
DR GO; GO:2000171; P:negative regulation of dendrite development; ISS:UniProtKB.
DR GO; GO:0010822; P:positive regulation of mitochondrion organization; ISS:UniProtKB.
DR GO; GO:0006626; P:protein targeting to mitochondrion; ISS:UniProtKB.
DR GO; GO:0010821; P:regulation of mitochondrion organization; ISS:UniProtKB.
DR GO; GO:0008090; P:retrograde axonal transport; ISS:UniProtKB.
DR InterPro; IPR026093; MGARP.
DR InterPro; IPR032773; MGARP_N.
DR PANTHER; PTHR22910; PTHR22910; 1.
DR Pfam; PF14962; AIF-MLS; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Mitochondrion outer membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..240
FT /note="Protein MGARP"
FT /id="PRO_0000318764"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8VI64"
FT TRANSMEM 41..63
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..240
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q8VI64"
FT REGION 166..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..223
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 128
FT /note="A -> T (in dbSNP:rs3208941)"
FT /id="VAR_051256"
FT CONFLICT 240
FT /note="G -> RANLQPVDISATNAIGCLISAFVFLVHLV (in Ref. 2;
FT AAG59896)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 240 AA; 25390 MW; 6E210FA627635CEC CRC64;
MYLRRAVSKT LALPLRAPPN PAPLGKDASL RRMSSNRFPG SSGSNMIYYL VVGVTVSAGG
YYAYKTVTSD QAKHTEHKTN LKEKTKAEIH PFQGEKENVA ETEKASSEAP EELIVEAEVV
DAEESPSATV VVIKEASACP GHVEAAPETT AVSAETGPEV TDAAARETTE VNPETTPEVT
NAALDEAVTI DNDKDTTKNE TSDEYAELEE ENSPAESESS AGDDLQEEAS VGSEAASAQG
