STRA6_RAT
ID STRA6_RAT Reviewed; 670 AA.
AC Q4QR83;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Receptor for retinol uptake STRA6;
DE AltName: Full=Retinol-binding protein receptor STRA6;
DE AltName: Full=Stimulated by retinoic acid gene 6 protein homolog;
GN Name=Stra6;
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 [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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).
CC -!- FUNCTION: Functions as retinol transporter. Accepts all-trans retinol
CC from the extracellular retinol-binding protein RBP4, facilitates
CC retinol transport across the cell membrane, and then transfers retinol
CC to the cytoplasmic retinol-binding protein RBP1. Retinol uptake is
CC enhanced by LRAT, an enzyme that converts retinol to all-trans retinyl
CC esters, the storage forms of vitamin A. Contributes to the activation
CC of a signaling cascade that depends on retinol transport and LRAT-
CC dependent generation of retinol metabolites that then trigger
CC activation of JAK2 and its target STAT5, and ultimately increase the
CC expression of SOCS3 and inhibit cellular responses to insulin.
CC Important for the homeostasis of vitamin A and its derivatives, such as
CC retinoic acid. STRA6-mediated transport is particularly important in
CC the eye, and under conditions of dietary vitamin A deficiency. Does not
CC transport retinoic acid. {ECO:0000250|UniProtKB:Q9BX79}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with JAK2 and STAT5.
CC Interacts (via extracellular domains) with RBP4. Interacts (via
CC cytoplasmic domains) with RBP1 (By similarity).
CC {ECO:0000250|UniProtKB:F1RAX4, ECO:0000250|UniProtKB:Q9BX79}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q0V8E7};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q0V8E7}. Note=In the
CC retinal pigment epithelium localizes to the basolateral membrane.
CC {ECO:0000250|UniProtKB:Q0V8E7}.
CC -!- DOMAIN: Contrary to predictions, contains nine transmembrane helices,
CC with an extracellular N-terminus and a cytoplasmic C-terminus (By
CC similarity). Besides, contains one long helix that dips into the
CC membrane and then runs more or less parallel to the membrane surface
CC (By similarity). {ECO:0000250|UniProtKB:F1RAX4,
CC ECO:0000250|UniProtKB:Q0V8E7}.
CC -!- PTM: Phosphorylated on tyrosine residues in response to RBP4 binding.
CC Phosphorylation requires the presence of LRAT, suggesting it may be
CC triggered by the uptake of retinol that is then metabolized within the
CC cell to retinoids that function as signaling molecules.
CC {ECO:0000250|UniProtKB:Q9BX79}.
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DR EMBL; BC097373; AAH97373.1; -; mRNA.
DR RefSeq; NP_001025095.1; NM_001029924.1.
DR AlphaFoldDB; Q4QR83; -.
DR SMR; Q4QR83; -.
DR STRING; 10116.ENSRNOP00000011074; -.
DR GlyGen; Q4QR83; 1 site.
DR PhosphoSitePlus; Q4QR83; -.
DR PaxDb; Q4QR83; -.
DR Ensembl; ENSRNOT00000011074; ENSRNOP00000011074; ENSRNOG00000008312.
DR GeneID; 363071; -.
DR KEGG; rno:363071; -.
DR UCSC; RGD:1307551; rat.
DR CTD; 64220; -.
DR RGD; 1307551; Stra6.
DR eggNOG; ENOG502QRSS; Eukaryota.
DR GeneTree; ENSGT00940000153246; -.
DR InParanoid; Q4QR83; -.
DR OrthoDB; 325169at2759; -.
DR PhylomeDB; Q4QR83; -.
DR TreeFam; TF331851; -.
DR Reactome; R-RNO-2453902; The canonical retinoid cycle in rods (twilight vision).
DR PRO; PR:Q4QR83; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000008312; Expressed in adult mammalian kidney and 13 other tissues.
DR ExpressionAtlas; Q4QR83; baseline and differential.
DR Genevisible; Q4QR83; RN.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR GO; GO:0034632; F:retinol transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0030325; P:adrenal gland development; ISO:RGD.
DR GO; GO:0061143; P:alveolar primary septum development; ISO:RGD.
DR GO; GO:0048844; P:artery morphogenesis; ISO:RGD.
DR GO; GO:0001568; P:blood vessel development; ISO:RGD.
DR GO; GO:0043010; P:camera-type eye development; ISS:UniProtKB.
DR GO; GO:0050890; P:cognition; ISO:RGD.
DR GO; GO:0048589; P:developmental growth; ISO:RGD.
DR GO; GO:0060539; P:diaphragm development; ISO:RGD.
DR GO; GO:0048546; P:digestive tract morphogenesis; ISO:RGD.
DR GO; GO:0097070; P:ductus arteriosus closure; ISO:RGD.
DR GO; GO:0043583; P:ear development; ISO:RGD.
DR GO; GO:0060900; P:embryonic camera-type eye formation; ISO:RGD.
DR GO; GO:0048566; P:embryonic digestive tract development; ISO:RGD.
DR GO; GO:0061029; P:eyelid development in camera-type eye; ISO:RGD.
DR GO; GO:0060325; P:face morphogenesis; ISO:RGD.
DR GO; GO:0007631; P:feeding behavior; ISO:RGD.
DR GO; GO:0030540; P:female genitalia development; ISO:RGD.
DR GO; GO:0060322; P:head development; ISO:RGD.
DR GO; GO:0060323; P:head morphogenesis; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0007612; P:learning; ISO:RGD.
DR GO; GO:0048286; P:lung alveolus development; ISO:RGD.
DR GO; GO:0030324; P:lung development; ISO:RGD.
DR GO; GO:0060426; P:lung vasculature development; ISO:RGD.
DR GO; GO:0050905; P:neuromuscular process; ISO:RGD.
DR GO; GO:0043585; P:nose morphogenesis; ISO:RGD.
DR GO; GO:0061205; P:paramesonephric duct development; ISO:RGD.
DR GO; GO:0048520; P:positive regulation of behavior; ISO:RGD.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISO:RGD.
DR GO; GO:0061156; P:pulmonary artery morphogenesis; ISO:RGD.
DR GO; GO:0003184; P:pulmonary valve morphogenesis; ISO:RGD.
DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR GO; GO:0034633; P:retinol transport; ISS:UniProtKB.
DR GO; GO:0048745; P:smooth muscle tissue development; ISO:RGD.
DR GO; GO:0061038; P:uterus morphogenesis; ISO:RGD.
DR GO; GO:0003281; P:ventricular septum development; ISO:RGD.
DR GO; GO:0071939; P:vitamin A import into cell; IBA:GO_Central.
DR GO; GO:0042297; P:vocal learning; ISO:RGD.
DR InterPro; IPR026612; STRA6.
DR PANTHER; PTHR21444:SF16; PTHR21444:SF16; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Retinol-binding; Transmembrane; Transmembrane helix;
KW Transport; Vitamin A.
FT CHAIN 1..670
FT /note="Receptor for retinol uptake STRA6"
FT /id="PRO_0000311231"
FT TOPO_DOM 1..50
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 72..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 120..144
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 166..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 190..205
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 227..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 318..368
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 390..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 445..474
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 496..510
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT INTRAMEM 511..548
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 549..670
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT REGION 235..294
FT /note="Interaction with RBP1"
FT /evidence="ECO:0000250|UniProtKB:Q9BX79"
FT MOD_RES 644
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9BX79"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 670 AA; 73763 MW; 4762A19CA3E816A6 CRC64;
MESQASENGS QTSSGVTDDY SSWYIEEPLG AEEVQPEGVN PLCQPTVPPA LHHACLASLS
LLALLLLALL VRRRRLWPHC AHCRPGLPSP VDFLAGNRSW TVPTAVFVAL FSNLCLLLPD
ENPLPFLNRT AASSPDGEPE TSRGPWKLLA LLYYPALYYP LAACATAGHR AAYLLGTVLS
WVHVSVQVWQ RAECPQDPKI YKHYSLLASL PLLLSLGFLS LWYPVQVVQS IRHRTGAGSQ
GLQTSYSEKY LRALLCPKKL DSCSHPASKR SLLSRAWAFS QHSIYTPEPG FCLPLKLVIS
ATLTGTATYQ VALLLLVSVV PTVQKVRAGI TTDVSYLLAG FGIVLSEDRQ EVVELVKHHL
WAVEACYISA LVLSCSLTFL LLIRSLRTHR ANLKALHRGA ALDLGPPLQS THPSRQAIVC
WMSFSAYQTA FSCLGLLVQQ VIFFLGTTIL AFLVFVPLLH GRNLLLLRSL ESTWPFWLTL
VLAVILQNIA ANWVFLESHH GYPELTNRRM LCVATFLLFP INMLVGAIMA IWRVLLSSLY
NTVHLGQMDL SLLPQRAASL DPGYHTYRNF LRIEASQSHP GVIAFCALLL HVPSPQPQPP
LAPQDSLRPA AEEEGMQLLQ TKDLMAKGAG PKGSRSRARW GLAYTLLHNP SLQAFRKAAL
TSAKANGTQP
