BORC6_MOUSE
ID BORC6_MOUSE Reviewed; 360 AA.
AC Q9D6W8; Q3TE21;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=BLOC-1-related complex subunit 6 {ECO:0000305};
GN Name=Borcs6 {ECO:0000312|MGI:MGI:1919173};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-41; SER-130; SER-173 AND
RP THR-201, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: As part of the BORC complex may play a role in lysosomes
CC movement and localization at the cell periphery. Associated with the
CC cytosolic face of lysosomes, the BORC complex may recruit ARL8B and
CC couple lysosomes to microtubule plus-end-directed kinesin motor.
CC {ECO:0000250|UniProtKB:Q96GS4}.
CC -!- SUBUNIT: Component of the BLOC-one-related complex (BORC) which is
CC composed of BLOC1S1, BLOC1S2, BORCS5, BORCS6, BORCS7, BORCS8, KXD1 and
CC SNAPIN. {ECO:0000250|UniProtKB:Q96GS4}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q96GS4}.
CC -!- SIMILARITY: Belongs to the BORCS6 family. {ECO:0000305}.
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DR EMBL; AK169875; BAE41427.1; -; mRNA.
DR EMBL; AK009886; BAB26563.1; -; mRNA.
DR EMBL; AK151629; BAE30563.1; -; mRNA.
DR EMBL; AL645902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS36190.1; -.
DR RefSeq; NP_082281.2; NM_028005.3.
DR AlphaFoldDB; Q9D6W8; -.
DR ComplexPortal; CPX-5061; BORC complex.
DR IntAct; Q9D6W8; 2.
DR MINT; Q9D6W8; -.
DR STRING; 10090.ENSMUSP00000059143; -.
DR iPTMnet; Q9D6W8; -.
DR PhosphoSitePlus; Q9D6W8; -.
DR EPD; Q9D6W8; -.
DR jPOST; Q9D6W8; -.
DR MaxQB; Q9D6W8; -.
DR PaxDb; Q9D6W8; -.
DR PeptideAtlas; Q9D6W8; -.
DR PRIDE; Q9D6W8; -.
DR ProteomicsDB; 273696; -.
DR Antibodypedia; 47971; 112 antibodies from 17 providers.
DR Ensembl; ENSMUST00000051888; ENSMUSP00000059143; ENSMUSG00000045176.
DR GeneID; 71923; -.
DR KEGG; mmu:71923; -.
DR UCSC; uc007jpb.1; mouse.
DR CTD; 54785; -.
DR MGI; MGI:1919173; Borcs6.
DR VEuPathDB; HostDB:ENSMUSG00000045176; -.
DR eggNOG; KOG4514; Eukaryota.
DR GeneTree; ENSGT00490000043453; -.
DR HOGENOM; CLU_782948_0_0_1; -.
DR InParanoid; Q9D6W8; -.
DR OMA; RHKDPAP; -.
DR OrthoDB; 1229804at2759; -.
DR PhylomeDB; Q9D6W8; -.
DR BioGRID-ORCS; 71923; 0 hits in 39 CRISPR screens.
DR ChiTaRS; Borcs6; mouse.
DR PRO; PR:Q9D6W8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9D6W8; protein.
DR Bgee; ENSMUSG00000045176; Expressed in granulocyte and 210 other tissues.
DR Genevisible; Q9D6W8; MM.
DR GO; GO:0099078; C:BORC complex; ISS:UniProtKB.
DR GO; GO:0098574; C:cytoplasmic side of lysosomal membrane; IC:ComplexPortal.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR GO; GO:0072384; P:organelle transport along microtubule; IC:ComplexPortal.
DR GO; GO:0051036; P:regulation of endosome size; IC:ComplexPortal.
DR GO; GO:0062196; P:regulation of lysosome size; IC:ComplexPortal.
DR InterPro; IPR019314; BORCS6.
DR PANTHER; PTHR13440; PTHR13440; 1.
DR Pfam; PF10157; BORCS6; 1.
PE 1: Evidence at protein level;
KW Lysosome; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..360
FT /note="BLOC-1-related complex subunit 6"
FT /id="PRO_0000393961"
FT REGION 1..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 201
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GS4"
FT CONFLICT 285
FT /note="L -> V (in Ref. 1; BAE41427)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="I -> T (in Ref. 1; BAE41427)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 38011 MW; C74C6ED72FF92EB0 CRC64;
MEAAQGRLGP EPELSVGAEH QAATFSGRPS RTPSKPPSVR TLSGEEEAES VGVSSRHPRA
SPKTWSGSIA HGPELDTWED KPSSRATPSG ARGRRGVPGS EHAPPPSSWY PEPEPSEDQP
SALRVCRRGS PGGVEMNVEL PQQEGDDDDD EDEEAAAGRA GRSFPSRLQD SRSLDGLSGA
CGGGGSSSSG ETGAGGGRRA TISSPLELEG TVSRHGDLTH FVANNLQLKI RLSGAPPPVP
PASVRPCLTP APTPTIPPID PDVLRDLERL SRELGGRVDR LLRGLGGAVQ ELTALSVGCI
QTYRDAVDSL GEAVDMSIKG MYTLLARCEE LERALQPVQG LARQVRDIRR TLEVLEALCK
