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Database: UniProt
Entry: D4ACC5_RAT
LinkDB: D4ACC5_RAT
Original site: D4ACC5_RAT 
ID   D4ACC5_RAT              Unreviewed;       560 AA.
AC   D4ACC5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 91.
DE   SubName: Full=Trafficking kinesin protein 1 {ECO:0000313|Ensembl:ENSRNOP00000026106.6};
GN   Name=Trak1 {ECO:0000313|Ensembl:ENSRNOP00000026106.6,
GN   ECO:0000313|RGD:1307844};
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 {ECO:0000313|Ensembl:ENSRNOP00000026106.6, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000026106.6, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000026106.6,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000026106.6}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000026106.6};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the milton family.
CC       {ECO:0000256|ARBA:ARBA00007007}.
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DR   AlphaFoldDB; D4ACC5; -.
DR   STRING; 10116.ENSRNOP00000026106; -.
DR   PaxDb; 10116-ENSRNOP00000026106; -.
DR   ABCD; D4ACC5; 1 sequenced antibody.
DR   Ensembl; ENSRNOT00000026106.6; ENSRNOP00000026106.6; ENSRNOG00000019262.7.
DR   AGR; RGD:1307844; -.
DR   RGD; 1307844; Trak1.
DR   eggNOG; KOG4360; Eukaryota.
DR   GeneTree; ENSGT00940000155697; -.
DR   HOGENOM; CLU_013450_0_0_1; -.
DR   InParanoid; D4ACC5; -.
DR   TreeFam; TF323495; -.
DR   Reactome; R-RNO-9013419; RHOT2 GTPase cycle.
DR   Reactome; R-RNO-9013425; RHOT1 GTPase cycle.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000019262; Expressed in skeletal muscle tissue and 19 other cell types or tissues.
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; ISO:RGD.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0005769; C:early endosome; ISO:RGD.
DR   GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR   GO; GO:0050811; F:GABA receptor binding; ISO:RGD.
DR   GO; GO:0017022; F:myosin binding; IBA:GO_Central.
DR   GO; GO:0030911; F:TPR domain binding; IDA:RGD.
DR   GO; GO:0098957; P:anterograde axonal transport of mitochondrion; ISO:RGD.
DR   GO; GO:0019896; P:axonal transport of mitochondrion; IMP:RGD.
DR   GO; GO:0048813; P:dendrite morphogenesis; IMP:RGD.
DR   GO; GO:0008333; P:endosome to lysosome transport; ISO:RGD.
DR   GO; GO:0048311; P:mitochondrion distribution; IBA:GO_Central.
DR   GO; GO:0022008; P:neurogenesis; IBA:GO_Central.
DR   GO; GO:0050772; P:positive regulation of axonogenesis; IMP:RGD.
DR   GO; GO:0006605; P:protein targeting; IBA:GO_Central.
DR   GO; GO:0047496; P:vesicle transport along microtubule; IBA:GO_Central.
DR   InterPro; IPR006933; HAP1_N.
DR   InterPro; IPR022154; TRAK1/2_C.
DR   PANTHER; PTHR15751; TRAFFICKING KINESIN-BINDING PROTEIN; 1.
DR   PANTHER; PTHR15751:SF11; TRAFFICKING KINESIN-BINDING PROTEIN 1; 1.
DR   Pfam; PF04849; HAP1_N; 1.
DR   Pfam; PF12448; Milton; 1.
DR   SMART; SM01424; HAP1_N; 1.
DR   SMART; SM01423; Milton; 1.
PE   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT   DOMAIN          1..249
FT                   /note="HAP1 N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01424"
FT   DOMAIN          308..477
FT                   /note="Trafficking kinesin-binding protein C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01423"
FT   COILED          8..63
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          152..249
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   560 AA;  63476 MW;  C4914ED6799ABC2C CRC64;
     MTKTYNDIDA VTRLLEEKER DLELAARIGQ SLLKKNKTLT ERNELLEEQV EHIREEVSQL
     RHELSMKDEL LQFYTSAAEE SEPESVCSTP LKRNESSSSV QNYFHLDSLQ KKLKDLEEEN
     VVLRSEACQL KTETITYEEK EQQLVNDCVK ELRDANVQIA SISEELAKKT EDAARQQEEI
     THLLSQIVDL QKKAKSCAVE NEELVQHLGA AKDAQRQLTA ELRELEDKYA ECMEMLHEAQ
     EELKNLRNKT MPTSRRYHSL GLFPMDSLAA EIEGTMRKEL QLEEPESPDI THQKRVFETV
     RNVNQVVKQR SLTPSPMNIP GSNQSSAMNS LLSSCVSTPR SSFYGSDVSH VVLDNKTNSI
     LLETEAADLG NEEHNKKPGT PGTPGSHDLE TALRRLSLRR ENYLSERRFF EEEQERKLRE
     LAEKGELHSG SLTPTESIMS LGTHSRFSEF TGFSGMSFSS RSYLPEKLQI VKPLEGSATL
     HHWQQLAQPH LGGILDPRPG VVTKGFRTLD VDLDEVYCLN DFEEDDTGDH ISLAGLATST
     TIQHMETSGR EAQLRPGSPW
//
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