STR6L_MOUSE
ID STR6L_MOUSE Reviewed; 621 AA.
AC Q9DBN1; B1AWX8; Q14DP6; Q14DS9; Q8C7I6;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Stimulated by retinoic acid gene 6 protein-like {ECO:0000312|MGI:MGI:1921402};
DE Short=STRA6-like protein {ECO:0000312|MGI:MGI:1921402};
DE AltName: Full=Retinol-binding protein 4 receptor 2 {ECO:0000303|PubMed:23105095};
DE Short=RBP4 receptor 2 {ECO:0000303|PubMed:23105095};
GN Name=Stra6l {ECO:0000312|MGI:MGI:1921402};
GN Synonyms=Rbpr2 {ECO:0000303|PubMed:23105095, ECO:0000312|MGI:MGI:1921402};
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 {ECO:0000312|EMBL:BAB23619.1};
RN [1] {ECO:0000312|EMBL:BAB23619.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB23619.1};
RC TISSUE=Liver {ECO:0000312|EMBL:BAB23619.1};
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] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
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] {ECO:0000312|EMBL:EDL02387.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAI12409.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-612, 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 [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP GLYCOSYLATION.
RX PubMed=23105095; DOI=10.1074/jbc.m112.369132;
RA Alapatt P., Guo F., Komanetsky S.M., Wang S., Cai J., Sargsyan A.,
RA Rodriguez Diaz E., Bacon B.T., Aryal P., Graham T.E.;
RT "Liver retinol transporter and receptor for serum retinol-binding protein
RT (RBP4).";
RL J. Biol. Chem. 288:1250-1265(2013).
CC -!- FUNCTION: Acts as a high-affinity cell-surface receptor for retinol-
CC binding protein RBP4 and mediates RBP4-dependent retinol uptake in the
CC liver. {ECO:0000269|PubMed:23105095}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23105095};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DBN1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DBN1-2; Sequence=VSP_058654;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver and small intestine. Also
CC expressed in spleen, kidney, colon, stomach, placenta, adipose tissue
CC and isolated adipocytes. {ECO:0000269|PubMed:23105095}.
CC -!- INDUCTION: Induced in adipose tissue after high fat diet. Down-
CC regulated by holo-RBP4, retinol and retinoic acid.
CC {ECO:0000269|PubMed:23105095}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:23105095}.
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; AK004855; BAB23619.1; -; mRNA.
DR EMBL; AK050348; BAC34204.1; -; mRNA.
DR EMBL; AK050152; BAC34096.1; -; mRNA.
DR EMBL; AL772381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466565; EDL02387.1; -; Genomic_DNA.
DR EMBL; BC112408; AAI12409.1; -; mRNA.
DR EMBL; BC111889; AAI11890.1; -; mRNA.
DR CCDS; CCDS18141.1; -. [Q9DBN1-1]
DR CCDS; CCDS80094.1; -. [Q9DBN1-2]
DR RefSeq; NP_001292350.1; NM_001305421.1. [Q9DBN1-2]
DR RefSeq; NP_083064.2; NM_028788.4. [Q9DBN1-1]
DR RefSeq; XP_006538375.1; XM_006538312.2. [Q9DBN1-1]
DR RefSeq; XP_006538376.1; XM_006538313.2. [Q9DBN1-2]
DR RefSeq; XP_006538377.1; XM_006538314.3. [Q9DBN1-2]
DR RefSeq; XP_006538378.1; XM_006538315.2. [Q9DBN1-2]
DR RefSeq; XP_017175902.1; XM_017320413.1.
DR AlphaFoldDB; Q9DBN1; -.
DR SMR; Q9DBN1; -.
DR STRING; 10090.ENSMUSP00000103412; -.
DR GlyGen; Q9DBN1; 1 site.
DR iPTMnet; Q9DBN1; -.
DR PhosphoSitePlus; Q9DBN1; -.
DR jPOST; Q9DBN1; -.
DR MaxQB; Q9DBN1; -.
DR PaxDb; Q9DBN1; -.
DR PRIDE; Q9DBN1; -.
DR ProteomicsDB; 254594; -. [Q9DBN1-1]
DR ProteomicsDB; 254595; -. [Q9DBN1-2]
DR Ensembl; ENSMUST00000030011; ENSMUSP00000030011; ENSMUSG00000028327. [Q9DBN1-1]
DR Ensembl; ENSMUST00000107782; ENSMUSP00000103411; ENSMUSG00000028327. [Q9DBN1-2]
DR Ensembl; ENSMUST00000107783; ENSMUSP00000103412; ENSMUSG00000028327. [Q9DBN1-1]
DR GeneID; 74152; -.
DR KEGG; mmu:74152; -.
DR UCSC; uc008ssz.3; mouse. [Q9DBN1-1]
DR CTD; 74152; -.
DR MGI; MGI:1921402; Stra6l.
DR VEuPathDB; HostDB:ENSMUSG00000028327; -.
DR eggNOG; KOG1105; Eukaryota.
DR GeneTree; ENSGT00940000153246; -.
DR InParanoid; Q9DBN1; -.
DR OMA; FTVPPWA; -.
DR OrthoDB; 1332509at2759; -.
DR PhylomeDB; Q9DBN1; -.
DR TreeFam; TF331851; -.
DR BioGRID-ORCS; 74152; 1 hit in 58 CRISPR screens.
DR ChiTaRS; Stra6l; mouse.
DR PRO; PR:Q9DBN1; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9DBN1; protein.
DR Bgee; ENSMUSG00000028327; Expressed in left lobe of liver and 46 other tissues.
DR Genevisible; Q8C7I6; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0034633; P:retinol transport; IGI:MGI.
DR GO; GO:0071939; P:vitamin A import into cell; IMP:MGI.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..621
FT /note="Stimulated by retinoic acid gene 6 protein-like"
FT /id="PRO_0000438364"
FT TOPO_DOM 1..21
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..110
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..173
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..321
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..424
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 498..621
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT MOD_RES 612
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..91
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_058654"
FT CONFLICT 21
FT /note="R -> G (in Ref. 1; BAC34096)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="G -> R (in Ref. 4; AAI11890)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="S -> G (in Ref. 3; EDL02387 and 4; AAI11890/
FT AAI12409)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 621 AA; 71003 MW; 909E1C6BC2A9EA60 CRC64;
MLAASTRTRQ INITCDNPVD REVFLHYSLI PSLCIILVLS FLQRREHRRQ RDDTSYLLGN
HFGIIVPLDF VGTFSNRWSY GAAFGATANK VMFLFSEGYQ PLTVPQWAQA FVLFIGGMEV
GLSYFPFFAC LSSEFQLVSS ILGFSYSLTW FVVTVLQISQ CPHGQFLGRF ETLVFYWPSL
LCLGFLLGRF LHMFLKALPV HLGLEPQTEE KSMLEAHQAK HVKQLLSKPR PQEGEKSWFQ
TRVYEWDPCF QFPSRMVGTL LLAFICLYLF IVIEFCVFLH VRDKLDMFED KLESYLTHMN
ETGTLTPIIL QVKELISVTK GVWVVTILPA ALTCVTYLFH ILACYRKHMK RLWAGDKHFL
PQKFHSPSSA ASVVAIARYS GWQIAYILWG YLIIHVVQSL CGVMLMYGLV LPIIHHRGLE
MLQGFGLGVL TLSIVVGLII LQVWIAGTFF LQPKLGTSDK QKPLALNNRR AFHNFNYFLF
FYNVLLGLGA CLSRLLISCL LGTWLIARID RTIMQSGYEG ADMGFGAWIG MLFVDHYHTN
PVLVSFCHIL ITSHKDRKLQ KTVKYWCLNQ SAGPRFSARA RTRWFLLQTL INNPRLVMLR
KSKSGHSSGE FTQILLTCSD C
