HUMMR_BOVIN
ID HUMMR_BOVIN Reviewed; 240 AA.
AC A6QLZ1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 71.
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=CESP1, HUMMR, OSAP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal spinal cord;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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, RHOT2/Miro-2, TRAK1/OIP106 and
CC TRAK2/GRIF1. {ECO:0000250|UniProtKB:Q8VI64}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8TDB4}.
CC Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q8VI64}; Single-
CC pass type IV membrane protein {ECO:0000250|UniProtKB:Q8VI64};
CC Cytoplasmic side {ECO:0000250|UniProtKB:Q8VI64}. Mitochondrion inner
CC membrane {ECO:0000250|UniProtKB:Q8VI64}; Single-pass type IV membrane
CC protein {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 -!- SEQUENCE CAUTION:
CC Sequence=AAI48138.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC148137; AAI48138.1; ALT_INIT; mRNA.
DR RefSeq; NP_001160083.1; NM_001166611.1.
DR AlphaFoldDB; A6QLZ1; -.
DR STRING; 9913.ENSBTAP00000045413; -.
DR PaxDb; A6QLZ1; -.
DR GeneID; 513234; -.
DR KEGG; bta:513234; -.
DR CTD; 84709; -.
DR eggNOG; ENOG502S6ZU; Eukaryota.
DR HOGENOM; CLU_088276_0_0_1; -.
DR InParanoid; A6QLZ1; -.
DR OrthoDB; 1339159at2759; -.
DR TreeFam; TF336324; -.
DR Proteomes; UP000009136; Unplaced.
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; ISS: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 2: Evidence at transcript 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_0000318763"
FT TOPO_DOM 1..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8VI64"
FT TRANSMEM 46..64
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..240
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q8VI64"
FT REGION 72..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 240 AA; 24888 MW; A770493CAFD58BF8 CRC64;
MYLRRAVSKT LALPLRAPPG PAPLRKDASL RWISSNKFPG SSGSNMIYYL VVGVTVSAGG
YYTYKRVTSG KAKRSDHVTD LKEKTKAELQ PPQGEKENLV GAEEASLEAP EVSSTEASPV
VTEDIPDAPA VVGKEAPPCP DDAEAAPSET VVVGAEPKPE MTDAATVETT EVSTETTSEV
TSTGPEEAAA VDSAEGTTEN ESPGECAELE ENSPVESESS AGEDLQEEAC AGSEAASAQG
