STRA6_PONAB
ID STRA6_PONAB Reviewed; 667 AA.
AC Q5R7B4; Q5RFR1;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 63.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5R7B4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5R7B4-2; Sequence=VSP_029440;
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; CR857091; CAH89396.1; -; mRNA.
DR EMBL; CR860204; CAH92346.1; -; mRNA.
DR RefSeq; NP_001127142.1; NM_001133670.1.
DR RefSeq; NP_001128855.1; NM_001135383.1. [Q5R7B4-1]
DR AlphaFoldDB; Q5R7B4; -.
DR SMR; Q5R7B4; -.
DR STRING; 9601.ENSPPYP00000007525; -.
DR GeneID; 100174192; -.
DR GeneID; 100189778; -.
DR KEGG; pon:100189778; -.
DR CTD; 64220; -.
DR eggNOG; ENOG502QRSS; Eukaryota.
DR InParanoid; Q5R7B4; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
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:0043010; P:camera-type eye development; ISS:UniProtKB.
DR GO; GO:0034633; P:retinol transport; ISS:UniProtKB.
DR InterPro; IPR026612; STRA6.
DR PANTHER; PTHR21444:SF16; PTHR21444:SF16; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Retinol-binding;
KW Transmembrane; Transmembrane helix; Transport; Vitamin A.
FT CHAIN 1..667
FT /note="Receptor for retinol uptake STRA6"
FT /id="PRO_0000311230"
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..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 317..367
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 389..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 444..473
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 495..509
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT INTRAMEM 510..547
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 548..667
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..293
FT /note="Interaction with RBP1"
FT /evidence="ECO:0000250|UniProtKB:Q9BX79"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 643
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9BX79"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 136..143
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_029440"
FT CONFLICT 233
FT /note="C -> R (in Ref. 1; CAH89396)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="R -> Q (in Ref. 1; CAH89396)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="S -> L (in Ref. 1; CAH89396)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="R -> H (in Ref. 1; CAH89396)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="S -> N (in Ref. 1; CAH89396)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 667 AA; 73567 MW; 1CA1699332BEE1BE CRC64;
MSSQPAGNQT SPGPTEDYSY GSWYIDEPQG GEELQPEGEV PSCHTSIPPS LYHACLASLS
ILVLLLLAML VRRRQLWPDC VRGRPGLPSP VDFLAGDRPQ AVPAAVFVVL FSSLCLLLPD
EDPLPFLTLA SAPSQDGKTE APRGAWKILG LFYYAALCYP LAACATAGHT AAHLLGSTLS
WAHLGVQVWQ RAECPQVPKI YKYYSLLASL PLLLGLGFLS LWYPVQLVRS FSCRTGAGSK
GLQSSYSEEY LRNLLCRKKL GSSSHTSKHG FLSWAWVCLR HCIYTPQPGF RLPLKLVLSA
TLTGTAIYQV ALLLLVGMVP NIQKVRAGVT TDVSYLLAGF GIVLSEDKQE VVELVKHHLW
ALEVCYISAL VLSCSLTFLV LMRSLVTHRT NLRALHRGAA LDSSPLHRSP HPSRRAIFCW
MSFSAYQTAF ICLGLLVQQI IFFLGTTALA FLVLMPVLHG RNLLLFRSLE SSWPFWLTLA
LAVILQSMAA HWVFLETHDG HPQLTNRRVL YAATFLLFPL NVLVGAMVAT WRVLLSALYN
AIHLGQMDLS LLPPRAATLD PGYYTYRNFL KIEVSQSHPA MTAFCSLLLQ ARSLLPRTMA
APQDSLRPGE EDEGMQLLQT KDSMAKGARP RANRGRARWG LAYTLLHNPT LQVFRKTALL
GANGAQP
