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Stimulated by retinoic acid gene 6 protein homolog

 STRA6_HUMAN             Reviewed;         667 AA.
Q9BX79; A8K7F1; B7Z5M9; B7Z862; D3DW54; F5GYI8; I3L1G8; Q6PJF8;
Q71RB9; Q7L9G1; Q7Z3U9; Q8TB21; Q9BX78; Q9H9U8;
04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
22-NOV-2017, entry version 115.
RecName: Full=Receptor for retinol uptake STRA6;
AltName: Full=Retinol-binding protein receptor STRA6 {ECO:0000303|PubMed:17503335, ECO:0000303|PubMed:22665496};
AltName: Full=Stimulated by retinoic acid gene 6 protein homolog;
Name=STRA6; ORFNames=PP14296, UNQ3126/PRO10282/PRO19578;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), INDUCTION, AND VARIANT
ILE-527.
PubMed=11358845;
Szeto W., Jiang W., Tice D.A., Rubinfeld B., Hollingshead P.G.,
Fong S.E., Dugger D.L., Pham T., Yansura D.G., Wong T.A.,
Grimaldi J.C., Corpuz R.T., Singh J.S., Frantz G.D., Devaux B.,
Crowley C.W., Schwall R.H., Eberhard D.A., Rastelli L., Polakis P.,
Pennica D.;
"Overexpression of the retinoic acid-responsive gene Stra6 in human
cancers and its synergistic induction by Wnt-1 and retinoic acid.";
Cancer Res. 61:4197-4205(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
ILE-527.
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Endometrium;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 5 AND 6), AND
VARIANT ILE-527.
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
SER-339.
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
SER-339.
TISSUE=Brain, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9452451;
Sundaram M., Sivaprasadarao A., DeSousa M.M., Findlay J.B.;
"The transfer of retinol from serum retinol-binding protein to
cellular retinol-binding protein is mediated by a membrane receptor.";
J. Biol. Chem. 273:3336-3342(1998).
[10]
INDUCTION.
PubMed=11832495; DOI=10.1074/jbc.M200334200;
Tice D.A., Szeto W., Soloviev I., Rubinfeld B., Fong S.E.,
Dugger D.L., Winer J., Williams P.M., Wieand D., Smith V.,
Schwall R.H., Pennica D., Polakis P.;
"Synergistic induction of tumor antigens by Wnt-1 signaling and
retinoic acid revealed by gene expression profiling.";
J. Biol. Chem. 277:14329-14335(2002).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18316031; DOI=10.1016/j.cmet.2008.01.009;
Isken A., Golczak M., Oberhauser V., Hunzelmann S., Driever W.,
Imanishi Y., Palczewski K., von Lintig J.;
"RBP4 disrupts vitamin A uptake homeostasis in a STRA6-deficient
animal model for Matthew-Wood syndrome.";
Cell Metab. 7:258-268(2008).
[12]
FUNCTION, INTERACTION WITH JAK2 AND STAT5, PHOSPHORYLATION AT TYR-643,
MUTAGENESIS OF TYR-643, AND CHARACTERIZATION OF VARIANT MCOPS9
MET-644.
PubMed=21368206; DOI=10.1073/pnas.1011115108;
Berry D.C., Jin H., Majumdar A., Noy N.;
"Signaling by vitamin A and retinol-binding protein regulates gene
expression to inhibit insulin responses.";
Proc. Natl. Acad. Sci. U.S.A. 108:4340-4345(2011).
[13]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RBP1 AND RBP4,
MUTAGENESIS OF LEU-255, AND PHOSPHORYLATION.
PubMed=22665496; DOI=10.1128/MCB.00505-12;
Berry D.C., O'Byrne S.M., Vreeland A.C., Blaner W.S., Noy N.;
"Cross talk between signaling and vitamin A transport by the retinol-
binding protein receptor STRA6.";
Mol. Cell. Biol. 32:3164-3175(2012).
[14]
INVOLVEMENT IN MCOPS9.
PubMed=17503335; DOI=10.1086/518177;
Golzio C., Martinovic-Bouriel J., Thomas S., Mougou-Zrelli S.,
Grattagliano-Bessieres B., Bonniere M., Delahaye S., Munnich A.,
Encha-Razavi F., Lyonnet S., Vekemans M., Attie-Bitach T.,
Etchevers H.C.;
"Matthew-Wood syndrome is caused by truncating mutations in the
retinol-binding protein receptor gene STRA6.";
Am. J. Hum. Genet. 80:1179-1187(2007).
[15]
VARIANTS MCOPS9 LEU-90; LEU-293; PRO-321; MET-644 AND CYS-655, AND
TISSUE SPECIFICITY.
PubMed=17273977; DOI=10.1086/512203;
Pasutto F., Sticht H., Hammersen G., Gillessen-Kaesbach G.,
FitzPatrick D.R., Nuernberg G., Brasch F., Schirmer-Zimmermann H.,
Tolmie J.L., Chitayat D., Houge G., Fernandez-Martinez L., Keating S.,
Mortier G., Hennekam R.C.M., von der Wense A., Slavotinek A.,
Meinecke P., Bitoun P., Becker C., Nuernberg P., Reis A., Rauch A.;
"Mutations in STRA6 cause a broad spectrum of malformations including
anophthalmia, congenital heart defects, diaphragmatic hernia, alveolar
capillary dysplasia, lung hypoplasia, and mental retardation.";
Am. J. Hum. Genet. 80:550-560(2007).
[16]
VARIANT ANOPHTHALMIA/MICROPHTHALMIA GLU-217.
PubMed=19112531;
White T., Lu T., Metlapally R., Katowitz J., Kherani F., Wang T.-Y.,
Tran-Viet K.-N., Young T.L.;
"Identification of STRA6 and SKI sequence variants in patients with
anophthalmia/microphthalmia.";
Mol. Vis. 14:2458-2465(2008).
[17]
VARIANTS ANOPHTHALMIA/MICROPHTHALMIA ARG-438 AND PRO-638.
PubMed=19309693; DOI=10.1002/humu.21023;
Chassaing N., Golzio C., Odent S., Lequeux L., Vigouroux A.,
Martinovic-Bouriel J., Tiziano F.D., Masini L., Piro F.,
Maragliano G., Delezoide A.-L., Attie-Bitach T., Manouvrier-Hanu S.,
Etchevers H.C., Calvas P.;
"Phenotypic spectrum of STRA6 mutations: from Matthew-Wood syndrome to
non-lethal anophthalmia.";
Hum. Mutat. 30:E673-E681(2009).
[18]
INVOLVEMENT IN ISOLATED COLOBOMATOUS MICROPHTHALMIA, VARIANT MCOPS9
LYS-304, CHARACTERIZATION OF VARIANT MCOPS9 LYS-304, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=21901792; DOI=10.1002/humu.21590;
Casey J., Kawaguchi R., Morrissey M., Sun H., McGettigan P.,
Nielsen J.E., Conroy J., Regan R., Kenny E., Cormican P., Morris D.W.,
Tormey P., Ni Chroinin M., Kennedy B.N., Lynch S., Green A., Ennis S.;
"First implication of STRA6 mutations in isolated anophthalmia,
microphthalmia, and coloboma: A new dimension to the STRA6
phenotype.";
Hum. Mutat. 32:1417-1426(2011).
-!- FUNCTION: Functions as retinol transporter. Accepts all-trans
retinol from the extracellular retinol-binding protein RBP4,
facilitates retinol transport across the cell membrane, and then
transfers retinol to the cytoplasmic retinol-binding protein RBP1
(PubMed:9452451, PubMed:18316031, PubMed:22665496). Retinol uptake
is enhanced by LRAT, an enzyme that converts retinol to all-trans
retinyl esters, the storage forms of vitamin A (PubMed:18316031,
PubMed:22665496). Contributes to the activation of a signaling
cascade that depends on retinol transport and LRAT-dependent
generation of retinol metabolites that then trigger activation of
JAK2 and its target STAT5, and ultimately increase the expression
of SOCS3 and inhibit cellular responses to insulin
(PubMed:21368206, PubMed:22665496). Important for the homeostasis
of vitamin A and its derivatives, such as retinoic acid
(PubMed:18316031). STRA6-mediated transport is particularly
important in the eye, and under conditions of dietary vitamin A
deficiency (Probable). Does not transport retinoic acid
(PubMed:18316031). {ECO:0000269|PubMed:18316031,
ECO:0000269|PubMed:21901792, ECO:0000269|PubMed:22665496,
ECO:0000269|PubMed:9452451, ECO:0000305}.
-!- SUBUNIT: Homodimer (By similarity). Interacts with JAK2 and STAT5
(PubMed:21368206). Interacts (via extracellular domains) with RBP4
(PubMed:22665496). Interacts (via cytoplasmic domains) with RBP1
(PubMed:22665496). {ECO:0000250|UniProtKB:F1RAX4,
ECO:0000269|PubMed:21368206, ECO:0000269|PubMed:22665496}.
-!- INTERACTION:
O76003:GLRX3; NbExp=4; IntAct=EBI-12140683, EBI-374781;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18316031,
ECO:0000269|PubMed:21901792, ECO:0000269|PubMed:9452451}; Multi-
pass membrane protein {ECO:0000305}. Note=In the retinal pigment
epithelium localizes to the basolateral membrane.
{ECO:0000250|UniProtKB:Q0V8E7}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=Q9BX79-1; Sequence=Displayed;
Name=2;
IsoId=Q9BX79-2; Sequence=VSP_029439;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9BX79-3; Sequence=VSP_029438;
Name=4;
IsoId=Q9BX79-4; Sequence=VSP_029437;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q9BX79-5; Sequence=VSP_046776;
Name=6;
IsoId=Q9BX79-6; Sequence=VSP_047497;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Broad expression. In adult eye expressed in
sclera, retina, retinal pigment epithelium, and trabecular
meshwork but not in choroid and iris.
{ECO:0000269|PubMed:17273977}.
-!- INDUCTION: Up-regulated in the colorectal cancer cell line WiDr by
the administration of retinoic acid and in tumors with frequent
defects in Wnt-1 signaling. {ECO:0000269|PubMed:11358845,
ECO:0000269|PubMed:11832495}.
-!- DOMAIN: Contrary to predictions, contains nine transmembrane
helices, with an extracellular N-terminus and a cytoplasmic C-
terminus (By similarity). Besides, contains one long helix that
dips into the membrane and then runs more or less parallel to the
membrane surface (By similarity). {ECO:0000250|UniProtKB:F1RAX4,
ECO:0000250|UniProtKB:Q0V8E7}.
-!- PTM: Phosphorylated on tyrosine residues in response to RBP4
binding (PubMed:21368206, PubMed:22665496). Phosphorylation
requires the presence of LRAT, suggesting it may be triggered by
the uptake of retinol that is then metabolized within the cell to
retinoids that function as signaling molecules (PubMed:22665496).
{ECO:0000269|PubMed:21368206, ECO:0000269|PubMed:22665496}.
-!- DISEASE: Microphthalmia, syndromic, 9 (MCOPS9) [MIM:601186]: A
rare clinical entity including as main characteristics
anophthalmia or severe microphthalmia, and pulmonary hypoplasia or
aplasia. Microphthalmia is a disorder of eye formation, ranging
from small size of a single eye to complete bilateral absence of
ocular tissues (anophthalmia). In many cases,
microphthalmia/anophthalmia occurs in association with syndromes
that include non-ocular abnormalities.
{ECO:0000269|PubMed:17273977, ECO:0000269|PubMed:17503335,
ECO:0000269|PubMed:21368206, ECO:0000269|PubMed:21901792}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Note=Mutations in STRA6 may be a cause of isolated
colobomatous microphthalmia, a disorder of the eye characterized
by an abnormally small ocular globe.
{ECO:0000269|PubMed:21901792}.
-!- SEQUENCE CAUTION:
Sequence=BAB14122.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAH13848.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAD97655.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF352728; AAK30289.1; -; mRNA.
EMBL; AF352729; AAK30290.1; -; mRNA.
EMBL; AY358748; AAQ89108.1; -; mRNA.
EMBL; AY359089; AAQ89447.1; -; mRNA.
EMBL; BX537413; CAD97655.1; ALT_INIT; mRNA.
EMBL; AK022603; BAB14122.1; ALT_INIT; mRNA.
EMBL; AK291966; BAF84655.1; -; mRNA.
EMBL; AK299191; BAH12965.1; -; mRNA.
EMBL; AK302932; BAH13848.1; ALT_INIT; mRNA.
EMBL; AF370419; AAQ15255.2; -; mRNA.
EMBL; AC023545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471136; EAW99353.1; -; Genomic_DNA.
EMBL; CH471136; EAW99356.1; -; Genomic_DNA.
EMBL; BC015881; AAH15881.1; -; mRNA.
EMBL; BC025256; AAH25256.1; -; mRNA.
CCDS; CCDS10261.1; -. [Q9BX79-1]
CCDS; CCDS45301.1; -. [Q9BX79-3]
CCDS; CCDS45302.1; -. [Q9BX79-2]
CCDS; CCDS55973.1; -. [Q9BX79-4]
CCDS; CCDS55974.1; -. [Q9BX79-5]
CCDS; CCDS58387.1; -. [Q9BX79-6]
RefSeq; NP_001136089.1; NM_001142617.1. [Q9BX79-1]
RefSeq; NP_001136090.1; NM_001142618.1. [Q9BX79-1]
RefSeq; NP_001136091.1; NM_001142619.1. [Q9BX79-3]
RefSeq; NP_001136092.1; NM_001142620.1. [Q9BX79-2]
RefSeq; NP_001185969.1; NM_001199040.1. [Q9BX79-5]
RefSeq; NP_001185970.1; NM_001199041.1. [Q9BX79-6]
RefSeq; NP_001185971.1; NM_001199042.1. [Q9BX79-4]
RefSeq; NP_071764.3; NM_022369.3. [Q9BX79-1]
RefSeq; XP_011520185.1; XM_011521883.1. [Q9BX79-1]
RefSeq; XP_016877968.1; XM_017022479.1. [Q9BX79-1]
UniGene; Hs.24553; -.
ProteinModelPortal; Q9BX79; -.
BioGrid; 122110; 2.
IntAct; Q9BX79; 2.
MINT; MINT-4722094; -.
STRING; 9606.ENSP00000456609; -.
TCDB; 2.A.90.1.3; the vitamin a receptor/transporter (stra6) family.
iPTMnet; Q9BX79; -.
PhosphoSitePlus; Q9BX79; -.
BioMuta; STRA6; -.
DMDM; 74733466; -.
EPD; Q9BX79; -.
MaxQB; Q9BX79; -.
PaxDb; Q9BX79; -.
PeptideAtlas; Q9BX79; -.
PRIDE; Q9BX79; -.
Ensembl; ENST00000323940; ENSP00000326085; ENSG00000137868. [Q9BX79-1]
Ensembl; ENST00000395105; ENSP00000378537; ENSG00000137868. [Q9BX79-1]
Ensembl; ENST00000423167; ENSP00000413012; ENSG00000137868. [Q9BX79-3]
Ensembl; ENST00000432245; ENSP00000407176; ENSG00000137868. [Q9BX79-2]
Ensembl; ENST00000449139; ENSP00000410221; ENSG00000137868. [Q9BX79-1]
Ensembl; ENST00000535552; ENSP00000440238; ENSG00000137868. [Q9BX79-5]
Ensembl; ENST00000563965; ENSP00000456609; ENSG00000137868. [Q9BX79-4]
Ensembl; ENST00000574278; ENSP00000458827; ENSG00000137868. [Q9BX79-6]
Ensembl; ENST00000616000; ENSP00000479112; ENSG00000137868. [Q9BX79-1]
GeneID; 64220; -.
KEGG; hsa:64220; -.
UCSC; uc002axj.5; human. [Q9BX79-1]
CTD; 64220; -.
DisGeNET; 64220; -.
EuPathDB; HostDB:ENSG00000137868.18; -.
GeneCards; STRA6; -.
HGNC; HGNC:30650; STRA6.
HPA; HPA040839; -.
MalaCards; STRA6; -.
MIM; 601186; phenotype.
MIM; 610745; gene.
neXtProt; NX_Q9BX79; -.
OpenTargets; ENSG00000137868; -.
Orphanet; 98938; Colobomatous microphthalmia.
Orphanet; 2470; Matthew-Wood syndrome.
PharmGKB; PA134956551; -.
eggNOG; ENOG410IDYH; Eukaryota.
eggNOG; ENOG410YGRH; LUCA.
GeneTree; ENSGT00390000015272; -.
HOVERGEN; HBG106311; -.
InParanoid; Q9BX79; -.
OMA; AIFCWMS; -.
OrthoDB; EOG091G05AQ; -.
PhylomeDB; Q9BX79; -.
TreeFam; TF331851; -.
Reactome; R-HSA-2453864; Retinoid cycle disease events.
Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision).
ChiTaRS; STRA6; human.
GenomeRNAi; 64220; -.
PRO; PR:Q9BX79; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000137868; -.
CleanEx; HS_STRA6; -.
ExpressionAtlas; Q9BX79; baseline and differential.
Genevisible; Q9BX79; HS.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043234; C:protein complex; IDA:LIFEdb.
GO; GO:0004872; F:receptor activity; IEA:InterPro.
GO; GO:0034632; F:retinol transporter activity; IDA:UniProtKB.
GO; GO:0030325; P:adrenal gland development; IMP:DFLAT.
GO; GO:0061143; P:alveolar primary septum development; IMP:DFLAT.
GO; GO:0048844; P:artery morphogenesis; IMP:DFLAT.
GO; GO:0001568; P:blood vessel development; IMP:DFLAT.
GO; GO:0043010; P:camera-type eye development; IMP:UniProtKB.
GO; GO:0050890; P:cognition; IMP:DFLAT.
GO; GO:0048589; P:developmental growth; IMP:DFLAT.
GO; GO:0060539; P:diaphragm development; IMP:DFLAT.
GO; GO:0048546; P:digestive tract morphogenesis; IMP:DFLAT.
GO; GO:0097070; P:ductus arteriosus closure; IMP:DFLAT.
GO; GO:0043583; P:ear development; IMP:DFLAT.
GO; GO:0060900; P:embryonic camera-type eye formation; IMP:DFLAT.
GO; GO:0048566; P:embryonic digestive tract development; IMP:DFLAT.
GO; GO:0061029; P:eyelid development in camera-type eye; IMP:DFLAT.
GO; GO:0060325; P:face morphogenesis; IMP:DFLAT.
GO; GO:0007631; P:feeding behavior; IMP:DFLAT.
GO; GO:0030540; P:female genitalia development; IMP:DFLAT.
GO; GO:0060322; P:head development; IMP:DFLAT.
GO; GO:0060323; P:head morphogenesis; IMP:DFLAT.
GO; GO:0007507; P:heart development; IMP:DFLAT.
GO; GO:0001822; P:kidney development; IMP:DFLAT.
GO; GO:0007612; P:learning; IMP:DFLAT.
GO; GO:0048286; P:lung alveolus development; IMP:DFLAT.
GO; GO:0030324; P:lung development; IMP:DFLAT.
GO; GO:0060426; P:lung vasculature development; IMP:DFLAT.
GO; GO:0050905; P:neuromuscular process; IMP:DFLAT.
GO; GO:0043585; P:nose morphogenesis; IMP:DFLAT.
GO; GO:0061205; P:paramesonephric duct development; IMP:DFLAT.
GO; GO:0048520; P:positive regulation of behavior; IMP:DFLAT.
GO; GO:0061156; P:pulmonary artery morphogenesis; IMP:DFLAT.
GO; GO:0003184; P:pulmonary valve morphogenesis; IMP:DFLAT.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0034633; P:retinol transport; IDA:UniProtKB.
GO; GO:0048745; P:smooth muscle tissue development; IMP:DFLAT.
GO; GO:0061038; P:uterus morphogenesis; IMP:DFLAT.
GO; GO:0003281; P:ventricular septum development; IMP:DFLAT.
GO; GO:0042297; P:vocal learning; IMP:DFLAT.
InterPro; IPR026612; STRA6.
PANTHER; PTHR21444:SF16; PTHR21444:SF16; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Disease mutation; Glycoprotein; Membrane; Microphthalmia;
Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Retinol-binding; Transmembrane; Transmembrane helix; Transport;
Vitamin A.
CHAIN 1 667 Receptor for retinol uptake STRA6.
/FTId=PRO_0000311228.
TOPO_DOM 1 50 Extracellular.
{ECO:0000250|UniProtKB:F1RAX4}.
TRANSMEM 51 71 Helical. {ECO:0000250|UniProtKB:F1RAX4}.
TOPO_DOM 72 100 Cytoplasmic.
{ECO:0000250|UniProtKB:F1RAX4}.
TRANSMEM 101 121 Helical. {ECO:0000250|UniProtKB:F1RAX4}.
TOPO_DOM 122 144 Extracellular.
{ECO:0000250|UniProtKB:F1RAX4}.
TRANSMEM 145 165 Helical. {ECO:0000250|UniProtKB:F1RAX4}.
TOPO_DOM 166 168 Cytoplasmic.
{ECO:0000250|UniProtKB:F1RAX4}.
TRANSMEM 169 189 Helical. {ECO:0000250|UniProtKB:F1RAX4}.
TOPO_DOM 190 205 Extracellular.
{ECO:0000250|UniProtKB:F1RAX4}.
TRANSMEM 206 226 Helical. {ECO:0000250|UniProtKB:F1RAX4}.
TOPO_DOM 227 295 Cytoplasmic.
{ECO:0000250|UniProtKB:F1RAX4}.
TRANSMEM 296 316 Helical. {ECO:0000250|UniProtKB:F1RAX4}.
TOPO_DOM 317 367 Extracellular.
{ECO:0000250|UniProtKB:F1RAX4}.
TRANSMEM 368 388 Helical. {ECO:0000250|UniProtKB:F1RAX4}.
TOPO_DOM 389 422 Cytoplasmic.
{ECO:0000250|UniProtKB:F1RAX4}.
TRANSMEM 423 443 Helical. {ECO:0000250|UniProtKB:F1RAX4}.
TOPO_DOM 444 473 Extracellular.
{ECO:0000250|UniProtKB:F1RAX4}.
TRANSMEM 474 494 Helical. {ECO:0000250|UniProtKB:F1RAX4}.
TOPO_DOM 495 509 Cytoplasmic.
{ECO:0000250|UniProtKB:F1RAX4}.
INTRAMEM 510 547 Helical. {ECO:0000250|UniProtKB:F1RAX4}.
TOPO_DOM 548 667 Cytoplasmic.
{ECO:0000250|UniProtKB:F1RAX4}.
REGION 235 293 Interaction with RBP1.
{ECO:0000269|PubMed:22665496}.
MOD_RES 643 643 Phosphotyrosine.
{ECO:0000269|PubMed:21368206}.
CARBOHYD 8 8 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 1 M -> MGGKGGGDTRGPVLFPCQLAQALSPRRAFPRELKEK
GQRM (in isoform 4).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_029437.
VAR_SEQ 1 1 M -> MQIRLLRAELVVPLWQFIRQWPPGSDGWGQMEEKGQ
RM (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046776.
VAR_SEQ 1 1 M -> MDSQGDWAAQEKGQRM (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047497.
VAR_SEQ 89 97 Missing (in isoform 3).
{ECO:0000303|PubMed:11358845,
ECO:0000303|PubMed:12975309}.
/FTId=VSP_029438.
VAR_SEQ 145 667 AWKILGLFYYAALYYPLAACATAGHTAAHLLGSTLSWAHLG
VQVWQRAECPQVPKIYKYYSLLASLPLLLGLGFLSLWYPVQ
LVRSFSRRTGAGSKGLQSSYSEEYLRNLLCRKKLGSSYHTS
KHGFLSWARVCLRHCIYTPQPGFHLPLKLVLSATLTGTAIY
QVALLLLVGVVPTIQKVRAGVTTDVSYLLAGFGIVLSEDKQ
EVVELVKHHLWALEVCYISALVLSCLLTFLVLMRSLVTHRT
NLRALHRGAALDLSPLHRSPHPSRQAIFCWMSFSAYQTAFI
CLGLLVQQIIFFLGTTALAFLVLMPVLHGRNLLLFRSLESS
WPFWLTLALAVILQNMAAHWVFLETHDGHPQLTNRRVLYAA
TFLLFPLNVLVGAMVATWRVLLSALYNAIHLGQMDLSLLPP
RAATLDPGYYTYRNFLKIEVSQSHPAMTAFCSLLLQAQSLL
PRTMAAPQDSLRPGEEDEGMQLLQTKDSMAKGARPGASRGR
ARWGLAYTLLHNPTLQVFRKTALLGANGAQP -> NLPKIT
ELRLVRAWI (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_029439.
VARIANT 90 90 P -> L (in MCOPS9; dbSNP:rs118203961).
{ECO:0000269|PubMed:17273977}.
/FTId=VAR_037168.
VARIANT 217 217 G -> E (in anophthalmia/microphthalmia).
{ECO:0000269|PubMed:19112531}.
/FTId=VAR_060203.
VARIANT 293 293 P -> L (in MCOPS9; dbSNP:rs118203958).
{ECO:0000269|PubMed:17273977}.
/FTId=VAR_037169.
VARIANT 304 304 G -> K (in MCOPS9; also found in a family
with isolated colobomatous
microphthalmia; affects STRA6 cell
surface expression and retinol uptake;
requires 2 nucleotide substitutions;
dbSNP:rs151341424).
{ECO:0000269|PubMed:21901792}.
/FTId=VAR_066849.
VARIANT 321 321 T -> P (in MCOPS9; dbSNP:rs118203962).
{ECO:0000269|PubMed:17273977}.
/FTId=VAR_037170.
VARIANT 339 339 G -> S (in dbSNP:rs17852249).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:15498874}.
/FTId=VAR_037171.
VARIANT 438 438 Q -> R (in anophthalmia/microphthalmia;
dbSNP:rs869025269).
{ECO:0000269|PubMed:19309693}.
/FTId=VAR_060204.
VARIANT 517 517 L -> F (in dbSNP:rs11545567).
/FTId=VAR_037172.
VARIANT 527 527 M -> I (in dbSNP:rs736118).
{ECO:0000269|PubMed:11358845,
ECO:0000269|PubMed:12975309,
ECO:0000269|PubMed:14702039}.
/FTId=VAR_037173.
VARIANT 638 638 R -> P (in anophthalmia/microphthalmia;
dbSNP:rs144691445).
{ECO:0000269|PubMed:19309693}.
/FTId=VAR_060205.
VARIANT 644 644 T -> M (in MCOPS9; loss of tyrosine
phosphorylation; dbSNP:rs118203960).
{ECO:0000269|PubMed:17273977,
ECO:0000269|PubMed:21368206}.
/FTId=VAR_037174.
VARIANT 655 655 R -> C (in MCOPS9; dbSNP:rs118203959).
{ECO:0000269|PubMed:17273977}.
/FTId=VAR_037175.
MUTAGEN 255 255 L->A: Loss of interaction with RBP1.
{ECO:0000269|PubMed:22665496}.
MUTAGEN 643 643 Y->F: Loss of tyrosine phosphorylation.
{ECO:0000269|PubMed:21368206}.
CONFLICT 95 95 A -> V (in Ref. 4; BAH12965).
{ECO:0000305}.
CONFLICT 408 408 R -> Q (in Ref. 3; CAD97655).
{ECO:0000305}.
CONFLICT 417 417 I -> M (in Ref. 4; BAH12965).
{ECO:0000305}.
CONFLICT 635 635 G -> S (in Ref. 4; BAH13848).
{ECO:0000305}.
SEQUENCE 667 AA; 73503 MW; D20840A46998BA2E CRC64;
MSSQPAGNQT SPGATEDYSY GSWYIDEPQG GEELQPEGEV PSCHTSIPPG LYHACLASLS
ILVLLLLAML VRRRQLWPDC VRGRPGLPSP VDFLAGDRPR AVPAAVFMVL LSSLCLLLPD
EDALPFLTLA SAPSQDGKTE APRGAWKILG LFYYAALYYP LAACATAGHT AAHLLGSTLS
WAHLGVQVWQ RAECPQVPKI YKYYSLLASL PLLLGLGFLS LWYPVQLVRS FSRRTGAGSK
GLQSSYSEEY LRNLLCRKKL GSSYHTSKHG FLSWARVCLR HCIYTPQPGF HLPLKLVLSA
TLTGTAIYQV ALLLLVGVVP TIQKVRAGVT TDVSYLLAGF GIVLSEDKQE VVELVKHHLW
ALEVCYISAL VLSCLLTFLV LMRSLVTHRT NLRALHRGAA LDLSPLHRSP HPSRQAIFCW
MSFSAYQTAF ICLGLLVQQI IFFLGTTALA FLVLMPVLHG RNLLLFRSLE SSWPFWLTLA
LAVILQNMAA HWVFLETHDG HPQLTNRRVL YAATFLLFPL NVLVGAMVAT WRVLLSALYN
AIHLGQMDLS LLPPRAATLD PGYYTYRNFL KIEVSQSHPA MTAFCSLLLQ AQSLLPRTMA
APQDSLRPGE EDEGMQLLQT KDSMAKGARP GASRGRARWG LAYTLLHNPT LQVFRKTALL
GANGAQP


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