TRAK2_RAT
ID TRAK2_RAT Reviewed; 913 AA.
AC Q8R2H7; Q8R2H6; Q8R4G3;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 21-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Trafficking kinesin-binding protein 2;
DE AltName: Full=Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 3 protein homolog;
DE AltName: Full=GABA-A receptor-interacting factor 1;
DE Short=GRIF-1;
DE AltName: Full=O-GlcNAc transferase-interacting protein of 98 kDa;
GN Name=Trak2; Synonyms=Als2cr3, Grif1, Oip98;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH GABA-A RECEPTOR.
RC TISSUE=Brain;
RX PubMed=12034717; DOI=10.1074/jbc.m200438200;
RA Beck M., Brickley K., Wilkinson H.L., Sharma S., Smith M., Chazot P.L.,
RA Pollard S., Stephenson F.A.;
RT "Identification, molecular cloning, and characterization of a novel GABAA
RT receptor-associated protein, GRIF-1.";
RL J. Biol. Chem. 277:30079-30090(2002).
RN [2]
RP SEQUENCE REVISION TO 579 AND 595-596, AND VARIANTS VAL-609 AND PRO-820.
RA Stephenson F.A.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH O-GLCNAC
RP TRANSFERASE, AND GLYCOSYLATION.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=12435728; DOI=10.1074/jbc.m209384200;
RA Iyer S.P.N., Akimoto Y., Hart G.W.;
RT "Identification and cloning of a novel family of coiled-coil domain
RT proteins that interact with O-GlcNAc transferase.";
RL J. Biol. Chem. 278:5399-5409(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 INTERACTION WITH HGS, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=17062640; DOI=10.1242/jcs.03249;
RA Kirk E., Chin L.S., Li L.;
RT "GRIF1 binds Hrs and is a new regulator of endosomal trafficking.";
RL J. Cell Sci. 119:4689-4701(2006).
RN [6]
RP SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: May regulate endosome-to-lysosome trafficking of membrane
CC cargo, including EGFR. {ECO:0000269|PubMed:17062640}.
CC -!- SUBUNIT: Interacts with RHOT1/Miro-1 and RHOT2/Miro-2 (By similarity).
CC Interacts with GABA-A receptor and O-GlcNAc transferase. Interacts with
CC HGS. {ECO:0000250, ECO:0000269|PubMed:12034717,
CC ECO:0000269|PubMed:12435728, ECO:0000269|PubMed:17062640}.
CC -!- INTERACTION:
CC Q8R2H7; Q12840: KIF5A; Xeno; NbExp=2; IntAct=EBI-1396483, EBI-713468;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Early endosome. Mitochondrion.
CC Note=Colocalizes with MGARP at the mitochondria. Translocates from the
CC cytoplasm to the mitochondria in a MGARP-dependent manner.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=GRIF-1a;
CC IsoId=Q8R2H7-1; Sequence=Displayed;
CC Name=2; Synonyms=GRIF-1b;
CC IsoId=Q8R2H7-2; Sequence=VSP_003786, VSP_003787;
CC -!- TISSUE SPECIFICITY: Present in heart and brain (at protein level).
CC {ECO:0000269|PubMed:17062640}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:12435728}.
CC -!- SIMILARITY: Belongs to the milton family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION: [Isoform 2]:
CC Sequence=AAL84588.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ288898; CAC81785.2; -; mRNA.
DR EMBL; AJ288898; CAC81786.2; -; mRNA.
DR EMBL; AF474163; AAL84588.1; ALT_FRAME; mRNA.
DR EMBL; BC088393; AAH88393.1; -; mRNA.
DR RefSeq; NP_598244.2; NM_133560.2. [Q8R2H7-1]
DR AlphaFoldDB; Q8R2H7; -.
DR SMR; Q8R2H7; -.
DR BioGRID; 251098; 5.
DR IntAct; Q8R2H7; 4.
DR MINT; Q8R2H7; -.
DR STRING; 10116.ENSRNOP00000015035; -.
DR iPTMnet; Q8R2H7; -.
DR PhosphoSitePlus; Q8R2H7; -.
DR PaxDb; Q8R2H7; -.
DR PRIDE; Q8R2H7; -.
DR ABCD; Q8R2H7; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000014939; ENSRNOP00000014939; ENSRNOG00000010881. [Q8R2H7-2]
DR Ensembl; ENSRNOT00000015034; ENSRNOP00000015035; ENSRNOG00000010881. [Q8R2H7-1]
DR GeneID; 171086; -.
DR KEGG; rno:171086; -.
DR UCSC; RGD:620915; rat. [Q8R2H7-1]
DR CTD; 66008; -.
DR RGD; 620915; Trak2.
DR eggNOG; KOG4360; Eukaryota.
DR GeneTree; ENSGT00940000158202; -.
DR HOGENOM; CLU_013450_0_1_1; -.
DR InParanoid; Q8R2H7; -.
DR OMA; RSKKACH; -.
DR OrthoDB; 1003820at2759; -.
DR PhylomeDB; Q8R2H7; -.
DR TreeFam; TF323495; -.
DR Reactome; R-RNO-9013419; RHOT2 GTPase cycle.
DR Reactome; R-RNO-9013425; RHOT1 GTPase cycle.
DR PRO; PR:Q8R2H7; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000010881; Expressed in Ammon's horn and 19 other tissues.
DR ExpressionAtlas; Q8R2H7; baseline and differential.
DR Genevisible; Q8R2H7; RN.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0044295; C:axonal growth cone; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0050811; F:GABA receptor binding; IDA:MGI.
DR GO; GO:0019894; F:kinesin binding; IDA:RGD.
DR GO; GO:0017022; F:myosin binding; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0030911; F:TPR domain binding; IDA:RGD.
DR GO; GO:0098957; P:anterograde axonal transport of mitochondrion; IBA:GO_Central.
DR GO; GO:0098972; P:anterograde dendritic transport of mitochondrion; ISO:RGD.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:RGD.
DR GO; GO:0098939; P:dendritic transport of mitochondrion; IMP:RGD.
DR GO; GO:0008333; P:endosome to lysosome transport; IDA:RGD.
DR GO; GO:0048311; P:mitochondrion distribution; IBA:GO_Central.
DR GO; GO:0050771; P:negative regulation of axonogenesis; IMP:RGD.
DR GO; GO:0022008; P:neurogenesis; IBA:GO_Central.
DR GO; GO:0006836; P:neurotransmitter transport; NAS:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:UniProtKB.
DR GO; GO:0006605; P:protein targeting; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0047496; P:vesicle transport along microtubule; IBA:GO_Central.
DR InterPro; IPR006933; HAP1_N.
DR InterPro; IPR022154; TRAK1/2_C.
DR Pfam; PF04849; HAP1_N; 1.
DR Pfam; PF12448; Milton; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Endosome; Glycoprotein;
KW Mitochondrion; Reference proteome; Transport.
FT CHAIN 1..913
FT /note="Trafficking kinesin-binding protein 2"
FT /id="PRO_0000064539"
FT DOMAIN 48..353
FT /note="HAP1 N-terminal"
FT REGION 11..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..507
FT /note="Interaction with HGS"
FT /evidence="ECO:0000269|PubMed:17062640"
FT REGION 442..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 134..355
FT /evidence="ECO:0000255"
FT COILED 502..519
FT /evidence="ECO:0000255"
FT COMPBIAS 11..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..787
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 653..672
FT /note="VATSNPGKCLSFTNSTFTFT -> ALVSHHCPVEAVRAVHPTRL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12034717,
FT ECO:0000303|PubMed:12435728"
FT /id="VSP_003786"
FT VAR_SEQ 673..913
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12034717,
FT ECO:0000303|PubMed:12435728"
FT /id="VSP_003787"
FT VARIANT 609
FT /note="E -> V"
FT /evidence="ECO:0000269|Ref.2"
FT VARIANT 820
FT /note="S -> P"
FT /evidence="ECO:0000269|Ref.2"
SQ SEQUENCE 913 AA; 101639 MW; D0E135DBEC30C28C CRC64;
MSLSQNAIFK SQTGEENLMS SNHRDSESIT DVCSNEDLPE VELVNLLEEQ LPQYKLRVDS
LFLYENQDWS QSSHQQQDAS ETLSPVLAEE TFRYMILGTD RVEQMTKTYN DIDMVTHLLA
ERDRDLELAA RIGQALLKRN HVLSEQNESL EEQLGQAFDQ VNQLQHELSK KEELLRIVSI
ASEESETDSS CSTPLRFNES FSLSQGLLQL DMMHEKLKEL EEENMALRSK ACHIKTETFT
YEEKEQKLIN DCVNELRETN AQMSRMTEEL SGKSDELLRY QEEISSLLSQ IVDLQHKLKE
HVIEKEELRL HLQASKDAQR QLTMELHELQ DRNMECLGML HESQEEIKEL RNKAGPSAHL
CFSQAYGVFA GESLAAEIEG TMRKKLSLDE ESVFKQKAQQ KRVFDTVKVA NDTRGRSVTF
PVLLPIPGSN RSSVIMTAKP FESGVQQTED KTLPNQGSST EVPGNSHPRD PPGLPEDSDL
ATALHRLSLR RQNYLSEKQF FAEEWERKLQ ILAEQEEEVS SCEALTENLA SFCTDQSETT
ELGSAGCLRG FMPEKLQIVK PLEGSQTLHH WQQLAQPNLG TILDPRPGVI TKGFTQMPKD
AVYHISDLEE DEEVGITFQV QQPLQLEQKP APPPPVTGIF LPPMTSAGGP VSVATSNPGK
CLSFTNSTFT FTTCRILHPS DITQVTPSSG FPSLSCGSSA GSASNTAVNS PAASYRLSIG
ESITNRRDST ITFSSTRSLA KLLQERGISA KVYHSPASEN PLLQLRPKAL ATPSTPPNSP
SQSPCSSPVP FEPRVHVSEN FLASRPAETF LQEMYGLRPS RAPPDVGQLK MNLVDRLKRL
GIARVVKTPV PRENGKSREA EMGLQKPDSA VYLNSGGSLL GGLRRNQSLP VMMGSFGAPV
CTTSPKMGIL KED
