XK_RAT
ID XK_RAT Reviewed; 445 AA.
AC Q5GH61;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Endoplasmic reticulum membrane adapter protein XK {ECO:0000305};
DE AltName: Full=Membrane transport protein XK;
DE AltName: Full=XK homolog;
DE AltName: Full=XK-related protein 1;
GN Name=Xk {ECO:0000312|RGD:1359650};
GN Synonyms=Xkh, Xkr1, Xrg1 {ECO:0000303|Ref.1};
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].
RC STRAIN=Sprague-Dawley;
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 [2]
RP PROTEIN SEQUENCE OF 410-415, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
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).
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:0000250|UniProtKB:P51811}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P51811}.
CC -!- SIMILARITY: Belongs to the XK family. {ECO:0000305}.
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DR EMBL; AY534256; AAT07105.1; -; mRNA.
DR RefSeq; NP_001012227.1; NM_001012227.1.
DR AlphaFoldDB; Q5GH61; -.
DR SMR; Q5GH61; -.
DR STRING; 10116.ENSRNOP00000039017; -.
DR iPTMnet; Q5GH61; -.
DR PhosphoSitePlus; Q5GH61; -.
DR PaxDb; Q5GH61; -.
DR PRIDE; Q5GH61; -.
DR GeneID; 497078; -.
DR KEGG; rno:497078; -.
DR UCSC; RGD:1359650; rat.
DR CTD; 7504; -.
DR RGD; 1359650; Xk.
DR eggNOG; ENOG502QTTF; Eukaryota.
DR InParanoid; Q5GH61; -.
DR PhylomeDB; Q5GH61; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR PRO; PR:Q5GH61; -.
DR Proteomes; UP000002494; Unplaced.
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; ISS: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; ISO:RGD.
DR GO; GO:0010961; P:cellular magnesium ion homeostasis; ISO:RGD.
DR GO; GO:0042552; P:myelination; ISO:RGD.
DR GO; GO:0031133; P:regulation of axon diameter; ISO:RGD.
DR GO; GO:0008361; P:regulation of cell size; ISO:RGD.
DR GO; GO:0048741; P:skeletal muscle fiber development; ISO:RGD.
DR InterPro; IPR018629; XK-rel.
DR Pfam; PF09815; XK-related; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..445
FT /note="Endoplasmic reticulum membrane adapter protein XK"
FT /id="PRO_0000190770"
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..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..207
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..276
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..348
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT DISULFID 346
FT /note="Interchain (with C-53 in Kell)"
FT /evidence="ECO:0000250|UniProtKB:P51811"
SQ SEQUENCE 445 AA; 51050 MW; 9C8C3B499692C072 CRC64;
MKFPASVLAS VFLFVAETMA ALYLSSTYRS AGDRMWQALT LFFSLMPCTL VQLTLLFVHR
DLSRDRPLVL LMHLLQLGPL YRCCEVFCIY CQSDQNEEPY VSITKKRQMP KDGLSEEVEK
EVGQSEGKLF THRSAFSRAS VIQAFLGSAP QLTLQLYITV LEQNITTGRF IMVLSLLSIV
YGALRCNILA IKIKYDEYEV KVKPLAYVCI FLWRSFEIAT RVIVLVLFTS VLKIWVVVVI
LVNFFSFFLY PWILFWNSGS PFPENIEKAL TRVGTTIVLG FLTLLYAGIN MFCWSAVQLK
IDNPELISKS QNWYRLLIYY MMRFVENSVL LLLWFFFKTD IYMYVCAPLL ILQLLIGYCT
SILFMLVFYQ FFHPCKKLFS SSVSESFSAC LRCVCWSSAR RKSTEPVGRI DTDLKACTDQ
GAQPSTSKLT PEATEIWTAV DLCST
