XK_MOUSE
ID XK_MOUSE Reviewed; 446 AA.
AC Q9QXY7;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Endoplasmic reticulum membrane adapter protein XK {ECO:0000305};
DE AltName: Full=Membrane transport protein XK {ECO:0000305};
DE AltName: Full=XK homolog {ECO:0000303|PubMed:10541802};
DE AltName: Full=XK-related protein 1 {ECO:0000303|PubMed:25231987};
GN Name=Xk {ECO:0000303|PubMed:10541802};
GN Synonyms=Xkh {ECO:0000303|PubMed:10541802},
GN Xkr1 {ECO:0000303|PubMed:25231987}, Xrg1 {ECO:0000303|Ref.2};
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Skeletal muscle;
RX PubMed=10541802; DOI=10.1007/s002510050681;
RA Collec E., Colin Y., Carbonnet F., Hattab C., Bertrand O., Cartron J.-P.,
RA Kim C.L.;
RT "Structure and expression of the mouse homologue of the XK gene.";
RL Immunogenetics 50:16-21(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Huang C.-H., Chen Y.;
RT "A superfamily of XK-related genes (XRG) widely expressed in vertebrates
RT and invertebrates.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
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 [4]
RP SUBUNIT.
RX PubMed=11132157; DOI=10.1007/s002510000251;
RA Lee S., Russo D.C., Pu J., Ho M., Redman C.M.;
RT "The mouse Kell blood group gene (Kel): cDNA sequence, genomic
RT organization, expression, and enzymatic function.";
RL Immunogenetics 52:53-62(2000).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=25231987; DOI=10.1074/jbc.m114.583419;
RA Suzuki J., Imanishi E., Nagata S.;
RT "Exposure of phosphatidylserine by Xk-related protein family members during
RT apoptosis.";
RL J. Biol. Chem. 289:30257-30267(2014).
CC -!- FUNCTION: Recruits the lipid transfer protein VPS13A from lipid
CC droplets to the endoplasmic reticulum (ER) membrane.
CC {ECO:0000250|UniProtKB:P51811}.
CC -!- SUBUNIT: Heterodimer with Kell; disulfide-linked. Interacts with
CC VPS13A. {ECO:0000250|UniProtKB:P51811}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:25231987}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P51811}.
CC -!- SIMILARITY: Belongs to the XK family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF155511; AAF14527.1; -; mRNA.
DR EMBL; AY534248; AAT07097.1; -; mRNA.
DR EMBL; AK007734; BAB25222.1; -; mRNA.
DR CCDS; CCDS30008.1; -.
DR RefSeq; NP_075989.1; NM_023500.2.
DR AlphaFoldDB; Q9QXY7; -.
DR SMR; Q9QXY7; -.
DR STRING; 10090.ENSMUSP00000015486; -.
DR ChEMBL; CHEMBL2176802; -.
DR PhosphoSitePlus; Q9QXY7; -.
DR SwissPalm; Q9QXY7; -.
DR MaxQB; Q9QXY7; -.
DR PaxDb; Q9QXY7; -.
DR PRIDE; Q9QXY7; -.
DR ProteomicsDB; 300003; -.
DR Antibodypedia; 10552; 162 antibodies from 26 providers.
DR DNASU; 22439; -.
DR Ensembl; ENSMUST00000015486; ENSMUSP00000015486; ENSMUSG00000015342.
DR GeneID; 22439; -.
DR KEGG; mmu:22439; -.
DR UCSC; uc009spq.1; mouse.
DR CTD; 7504; -.
DR MGI; MGI:103569; Xk.
DR VEuPathDB; HostDB:ENSMUSG00000015342; -.
DR eggNOG; ENOG502QTTF; Eukaryota.
DR GeneTree; ENSGT00390000003231; -.
DR HOGENOM; CLU_037429_1_1_1; -.
DR InParanoid; Q9QXY7; -.
DR OMA; ICVLQQE; -.
DR OrthoDB; 768086at2759; -.
DR PhylomeDB; Q9QXY7; -.
DR TreeFam; TF331465; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR BioGRID-ORCS; 22439; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q9QXY7; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9QXY7; protein.
DR Bgee; ENSMUSG00000015342; Expressed in hindlimb stylopod muscle and 67 other tissues.
DR ExpressionAtlas; Q9QXY7; baseline and differential.
DR Genevisible; Q9QXY7; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISS:UniProtKB.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IGI:MGI.
DR GO; GO:0010961; P:cellular magnesium ion homeostasis; IGI:MGI.
DR GO; GO:0042552; P:myelination; IMP:MGI.
DR GO; GO:0031133; P:regulation of axon diameter; IGI:MGI.
DR GO; GO:0008361; P:regulation of cell size; IGI:MGI.
DR GO; GO:0048741; P:skeletal muscle fiber development; IGI:MGI.
DR InterPro; IPR018629; XK-rel.
DR Pfam; PF09815; XK-related; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Disulfide bond; Endoplasmic reticulum; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..446
FT /note="Endoplasmic reticulum membrane adapter protein XK"
FT /id="PRO_0000190768"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..37
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..140
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..208
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..349
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5GH61"
FT DISULFID 347
FT /note="Interchain (with C-53 in Kell)"
FT /evidence="ECO:0000250|UniProtKB:P51811"
SQ SEQUENCE 446 AA; 51115 MW; D785FB7B9E28B98B CRC64;
MKFPASVIAS VFLFVAETAA ALYLSSTYRS AGDRMWQVLT LLFSLMPCAL VQFTLLFVHR
DLSRDRPLAL LMHLLQLGPL YRCCEVFCIY CQSDQNEEPY VSITKKRQMP KDGLSEEVEK
EVGQAEGKLI THRSAFSRAS VIQAFLGSAP QLTLQLYITV LEQNITTGRC FIMTLSLLSI
VYGALRCNIL AIKIKYDEYE VKVKPLAYVC IFLWRSFEIA TRVIVLVLFT SVLKIWVVAV
ILVNFFSFFL YPWIVFWCSG SPFPENIEKA LSRVGTTIVL CFLTLLYAGI NMFCWSAVQL
KIDNPELISK SQNWYRLLIY YMTRFIENSV LLLLWYFFKT DIYMYVCAPL LILQLLIGYC
TGILFMLVFY QFFHPCKKLF SSSVSESFRA LLRCACWSSL RRKSSEPVGR IDTDLKACTE
QDVMPTTSKV IPEATDIWTA VDLCSA
