STRA6_HUMAN
ID STRA6_HUMAN Reviewed; 667 AA.
AC Q9BX79; A8K7F1; B7Z5M9; B7Z862; D3DW54; F5GYI8; I3L1G8; Q6PJF8; Q71RB9;
AC Q7L9G1; Q7Z3U9; Q8TB21; Q9BX78; Q9H9U8;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Receptor for retinol uptake STRA6;
DE AltName: Full=Retinol-binding protein receptor STRA6 {ECO:0000303|PubMed:17503335, ECO:0000303|PubMed:22665496};
DE AltName: Full=Stimulated by retinoic acid gene 6 protein homolog;
GN Name=STRA6; ORFNames=PP14296, UNQ3126/PRO10282/PRO19578;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), INDUCTION, AND VARIANT
RP ILE-527.
RX PubMed=11358845;
RA Szeto W., Jiang W., Tice D.A., Rubinfeld B., Hollingshead P.G., Fong S.E.,
RA Dugger D.L., Pham T., Yansura D.G., Wong T.A., Grimaldi J.C., Corpuz R.T.,
RA Singh J.S., Frantz G.D., Devaux B., Crowley C.W., Schwall R.H.,
RA Eberhard D.A., Rastelli L., Polakis P., Pennica D.;
RT "Overexpression of the retinoic acid-responsive gene Stra6 in human cancers
RT and its synergistic induction by Wnt-1 and retinoic acid.";
RL Cancer Res. 61:4197-4205(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP ILE-527.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Endometrium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 5 AND 6), AND VARIANT
RP ILE-527.
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-339.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP SER-339.
RC TISSUE=Brain, and Muscle;
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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9452451; DOI=10.1074/jbc.273.6.3336;
RA Sundaram M., Sivaprasadarao A., DeSousa M.M., Findlay J.B.;
RT "The transfer of retinol from serum retinol-binding protein to cellular
RT retinol-binding protein is mediated by a membrane receptor.";
RL J. Biol. Chem. 273:3336-3342(1998).
RN [10]
RP INDUCTION.
RX PubMed=11832495; DOI=10.1074/jbc.m200334200;
RA Tice D.A., Szeto W., Soloviev I., Rubinfeld B., Fong S.E., Dugger D.L.,
RA Winer J., Williams P.M., Wieand D., Smith V., Schwall R.H., Pennica D.,
RA Polakis P.;
RT "Synergistic induction of tumor antigens by Wnt-1 signaling and retinoic
RT acid revealed by gene expression profiling.";
RL J. Biol. Chem. 277:14329-14335(2002).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18316031; DOI=10.1016/j.cmet.2008.01.009;
RA Isken A., Golczak M., Oberhauser V., Hunzelmann S., Driever W.,
RA Imanishi Y., Palczewski K., von Lintig J.;
RT "RBP4 disrupts vitamin A uptake homeostasis in a STRA6-deficient animal
RT model for Matthew-Wood syndrome.";
RL Cell Metab. 7:258-268(2008).
RN [12]
RP FUNCTION, INTERACTION WITH JAK2 AND STAT5, PHOSPHORYLATION AT TYR-643,
RP MUTAGENESIS OF TYR-643, AND CHARACTERIZATION OF VARIANT MCOPS9 MET-644.
RX PubMed=21368206; DOI=10.1073/pnas.1011115108;
RA Berry D.C., Jin H., Majumdar A., Noy N.;
RT "Signaling by vitamin A and retinol-binding protein regulates gene
RT expression to inhibit insulin responses.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:4340-4345(2011).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RBP1 AND RBP4, MUTAGENESIS
RP OF LEU-255, AND PHOSPHORYLATION.
RX PubMed=22665496; DOI=10.1128/mcb.00505-12;
RA Berry D.C., O'Byrne S.M., Vreeland A.C., Blaner W.S., Noy N.;
RT "Cross talk between signaling and vitamin A transport by the retinol-
RT binding protein receptor STRA6.";
RL Mol. Cell. Biol. 32:3164-3175(2012).
RN [14]
RP INVOLVEMENT IN MCOPS9.
RX PubMed=17503335; DOI=10.1086/518177;
RA Golzio C., Martinovic-Bouriel J., Thomas S., Mougou-Zrelli S.,
RA Grattagliano-Bessieres B., Bonniere M., Delahaye S., Munnich A.,
RA Encha-Razavi F., Lyonnet S., Vekemans M., Attie-Bitach T., Etchevers H.C.;
RT "Matthew-Wood syndrome is caused by truncating mutations in the retinol-
RT binding protein receptor gene STRA6.";
RL Am. J. Hum. Genet. 80:1179-1187(2007).
RN [15]
RP VARIANTS MCOPS9 LEU-90; LEU-293; PRO-321; MET-644 AND CYS-655, AND TISSUE
RP SPECIFICITY.
RX PubMed=17273977; DOI=10.1086/512203;
RA Pasutto F., Sticht H., Hammersen G., Gillessen-Kaesbach G.,
RA FitzPatrick D.R., Nuernberg G., Brasch F., Schirmer-Zimmermann H.,
RA Tolmie J.L., Chitayat D., Houge G., Fernandez-Martinez L., Keating S.,
RA Mortier G., Hennekam R.C.M., von der Wense A., Slavotinek A., Meinecke P.,
RA Bitoun P., Becker C., Nuernberg P., Reis A., Rauch A.;
RT "Mutations in STRA6 cause a broad spectrum of malformations including
RT anophthalmia, congenital heart defects, diaphragmatic hernia, alveolar
RT capillary dysplasia, lung hypoplasia, and mental retardation.";
RL Am. J. Hum. Genet. 80:550-560(2007).
RN [16]
RP VARIANT ANOPHTHALMIA/MICROPHTHALMIA GLU-217.
RX PubMed=19112531;
RA White T., Lu T., Metlapally R., Katowitz J., Kherani F., Wang T.-Y.,
RA Tran-Viet K.-N., Young T.L.;
RT "Identification of STRA6 and SKI sequence variants in patients with
RT anophthalmia/microphthalmia.";
RL Mol. Vis. 14:2458-2465(2008).
RN [17]
RP VARIANTS ANOPHTHALMIA/MICROPHTHALMIA ARG-438 AND PRO-638.
RX PubMed=19309693; DOI=10.1002/humu.21023;
RA Chassaing N., Golzio C., Odent S., Lequeux L., Vigouroux A.,
RA Martinovic-Bouriel J., Tiziano F.D., Masini L., Piro F., Maragliano G.,
RA Delezoide A.-L., Attie-Bitach T., Manouvrier-Hanu S., Etchevers H.C.,
RA Calvas P.;
RT "Phenotypic spectrum of STRA6 mutations: from Matthew-Wood syndrome to non-
RT lethal anophthalmia.";
RL Hum. Mutat. 30:E673-E681(2009).
RN [18]
RP INVOLVEMENT IN ISOLATED COLOBOMATOUS MICROPHTHALMIA, VARIANT MCOPS9
RP LYS-304, CHARACTERIZATION OF VARIANT MCOPS9 LYS-304, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21901792; DOI=10.1002/humu.21590;
RA Casey J., Kawaguchi R., Morrissey M., Sun H., McGettigan P., Nielsen J.E.,
RA Conroy J., Regan R., Kenny E., Cormican P., Morris D.W., Tormey P.,
RA Ni Chroinin M., Kennedy B.N., Lynch S., Green A., Ennis S.;
RT "First implication of STRA6 mutations in isolated anophthalmia,
RT microphthalmia, and coloboma: A new dimension to the STRA6 phenotype.";
RL Hum. Mutat. 32:1417-1426(2011).
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 (PubMed:9452451,
CC PubMed:18316031, PubMed:22665496). Retinol uptake is enhanced by LRAT,
CC an enzyme that converts retinol to all-trans retinyl esters, the
CC storage forms of vitamin A (PubMed:18316031, PubMed:22665496).
CC Contributes to the activation of a signaling cascade that depends on
CC retinol transport and LRAT-dependent generation of retinol metabolites
CC that then trigger activation of JAK2 and its target STAT5, and
CC ultimately increase the expression of SOCS3 and inhibit cellular
CC responses to insulin (PubMed:21368206, PubMed:22665496). Important for
CC the homeostasis of vitamin A and its derivatives, such as retinoic acid
CC (PubMed:18316031). STRA6-mediated transport is particularly important
CC in the eye, and under conditions of dietary vitamin A deficiency
CC (Probable). Does not transport retinoic acid (PubMed:18316031).
CC {ECO:0000269|PubMed:18316031, ECO:0000269|PubMed:21901792,
CC ECO:0000269|PubMed:22665496, ECO:0000269|PubMed:9452451, ECO:0000305}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with JAK2 and STAT5
CC (PubMed:21368206). Interacts (via extracellular domains) with RBP4
CC (PubMed:22665496). Interacts (via cytoplasmic domains) with RBP1
CC (PubMed:22665496). {ECO:0000250|UniProtKB:F1RAX4,
CC ECO:0000269|PubMed:21368206, ECO:0000269|PubMed:22665496}.
CC -!- INTERACTION:
CC Q9BX79-6; O76003: GLRX3; NbExp=3; IntAct=EBI-12140683, EBI-374781;
CC Q9BX79-6; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-12140683, EBI-12012928;
CC Q9BX79-6; Q5TA81: LCE2C; NbExp=3; IntAct=EBI-12140683, EBI-11973993;
CC Q9BX79-6; P17568: NDUFB7; NbExp=3; IntAct=EBI-12140683, EBI-1246238;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18316031,
CC ECO:0000269|PubMed:21901792, ECO:0000269|PubMed:9452451}; Multi-pass
CC membrane protein {ECO:0000305}. Note=In the retinal pigment epithelium
CC localizes to the basolateral membrane. {ECO:0000250|UniProtKB:Q0V8E7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q9BX79-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BX79-2; Sequence=VSP_029439;
CC Name=3;
CC IsoId=Q9BX79-3; Sequence=VSP_029438;
CC Name=4;
CC IsoId=Q9BX79-4; Sequence=VSP_029437;
CC Name=5;
CC IsoId=Q9BX79-5; Sequence=VSP_046776;
CC Name=6;
CC IsoId=Q9BX79-6; Sequence=VSP_047497;
CC -!- TISSUE SPECIFICITY: Broad expression. In adult eye expressed in sclera,
CC retina, retinal pigment epithelium, and trabecular meshwork but not in
CC choroid and iris. {ECO:0000269|PubMed:17273977}.
CC -!- INDUCTION: Up-regulated in the colorectal cancer cell line WiDr by the
CC administration of retinoic acid and in tumors with frequent defects in
CC Wnt-1 signaling. {ECO:0000269|PubMed:11358845,
CC ECO:0000269|PubMed:11832495}.
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 (PubMed:21368206, PubMed:22665496). Phosphorylation requires the
CC presence of LRAT, suggesting it may be triggered by the uptake of
CC retinol that is then metabolized within the cell to retinoids that
CC function as signaling molecules (PubMed:22665496).
CC {ECO:0000269|PubMed:21368206, ECO:0000269|PubMed:22665496}.
CC -!- DISEASE: Microphthalmia, syndromic, 9 (MCOPS9) [MIM:601186]: A rare
CC clinical entity including as main characteristics anophthalmia or
CC severe microphthalmia, and pulmonary hypoplasia or aplasia.
CC Microphthalmia is a disorder of eye formation, ranging from small size
CC of a single eye to complete bilateral absence of ocular tissues
CC (anophthalmia). In many cases, microphthalmia/anophthalmia occurs in
CC association with syndromes that include non-ocular abnormalities.
CC {ECO:0000269|PubMed:17273977, ECO:0000269|PubMed:17503335,
CC ECO:0000269|PubMed:21368206, ECO:0000269|PubMed:21901792}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Note=Mutations in STRA6 may be a cause of isolated
CC colobomatous microphthalmia, a disorder of the eye characterized by an
CC abnormally small ocular globe. {ECO:0000269|PubMed:21901792}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14122.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAH13848.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD97655.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF352728; AAK30289.1; -; mRNA.
DR EMBL; AF352729; AAK30290.1; -; mRNA.
DR EMBL; AY358748; AAQ89108.1; -; mRNA.
DR EMBL; AY359089; AAQ89447.1; -; mRNA.
DR EMBL; BX537413; CAD97655.1; ALT_INIT; mRNA.
DR EMBL; AK022603; BAB14122.1; ALT_INIT; mRNA.
DR EMBL; AK291966; BAF84655.1; -; mRNA.
DR EMBL; AK299191; BAH12965.1; -; mRNA.
DR EMBL; AK302932; BAH13848.1; ALT_INIT; mRNA.
DR EMBL; AF370419; AAQ15255.2; -; mRNA.
DR EMBL; AC023545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471136; EAW99353.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99356.1; -; Genomic_DNA.
DR EMBL; BC015881; AAH15881.1; -; mRNA.
DR EMBL; BC025256; AAH25256.1; -; mRNA.
DR CCDS; CCDS10261.1; -. [Q9BX79-1]
DR CCDS; CCDS45301.1; -. [Q9BX79-3]
DR CCDS; CCDS45302.1; -. [Q9BX79-2]
DR CCDS; CCDS55973.1; -. [Q9BX79-4]
DR CCDS; CCDS55974.1; -. [Q9BX79-5]
DR CCDS; CCDS58387.1; -. [Q9BX79-6]
DR RefSeq; NP_001136089.1; NM_001142617.1. [Q9BX79-1]
DR RefSeq; NP_001136090.1; NM_001142618.1. [Q9BX79-1]
DR RefSeq; NP_001136091.1; NM_001142619.1. [Q9BX79-3]
DR RefSeq; NP_001136092.1; NM_001142620.1. [Q9BX79-2]
DR RefSeq; NP_001185969.1; NM_001199040.1. [Q9BX79-5]
DR RefSeq; NP_001185970.1; NM_001199041.1. [Q9BX79-6]
DR RefSeq; NP_001185971.1; NM_001199042.1. [Q9BX79-4]
DR RefSeq; NP_071764.3; NM_022369.3. [Q9BX79-1]
DR RefSeq; XP_011520185.1; XM_011521883.1. [Q9BX79-1]
DR RefSeq; XP_016877968.1; XM_017022479.1. [Q9BX79-1]
DR AlphaFoldDB; Q9BX79; -.
DR SMR; Q9BX79; -.
DR BioGRID; 122110; 33.
DR IntAct; Q9BX79; 7.
DR STRING; 9606.ENSP00000456609; -.
DR DrugBank; DB00162; Vitamin A.
DR TCDB; 2.A.90.1.3; the vitamin a receptor/transporter (stra6) family.
DR GlyGen; Q9BX79; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BX79; -.
DR PhosphoSitePlus; Q9BX79; -.
DR BioMuta; STRA6; -.
DR DMDM; 74733466; -.
DR EPD; Q9BX79; -.
DR jPOST; Q9BX79; -.
DR MassIVE; Q9BX79; -.
DR MaxQB; Q9BX79; -.
DR PaxDb; Q9BX79; -.
DR PeptideAtlas; Q9BX79; -.
DR PRIDE; Q9BX79; -.
DR ProteomicsDB; 24753; -.
DR ProteomicsDB; 46637; -.
DR ProteomicsDB; 79375; -. [Q9BX79-1]
DR ProteomicsDB; 79376; -. [Q9BX79-2]
DR ProteomicsDB; 79377; -. [Q9BX79-3]
DR ProteomicsDB; 79378; -. [Q9BX79-4]
DR Antibodypedia; 26878; 267 antibodies from 32 providers.
DR DNASU; 64220; -.
DR Ensembl; ENST00000323940.9; ENSP00000326085.5; ENSG00000137868.19. [Q9BX79-1]
DR Ensembl; ENST00000395105.9; ENSP00000378537.4; ENSG00000137868.19. [Q9BX79-1]
DR Ensembl; ENST00000423167.6; ENSP00000413012.2; ENSG00000137868.19. [Q9BX79-3]
DR Ensembl; ENST00000432245.6; ENSP00000407176.2; ENSG00000137868.19. [Q9BX79-2]
DR Ensembl; ENST00000449139.6; ENSP00000410221.2; ENSG00000137868.19. [Q9BX79-1]
DR Ensembl; ENST00000535552.5; ENSP00000440238.1; ENSG00000137868.19. [Q9BX79-5]
DR Ensembl; ENST00000563965.5; ENSP00000456609.1; ENSG00000137868.19. [Q9BX79-4]
DR Ensembl; ENST00000574278.5; ENSP00000458827.1; ENSG00000137868.19. [Q9BX79-6]
DR Ensembl; ENST00000616000.4; ENSP00000479112.1; ENSG00000137868.19. [Q9BX79-1]
DR Ensembl; ENST00000672446.1; ENSP00000500590.1; ENSG00000288257.1. [Q9BX79-3]
DR Ensembl; ENST00000672526.1; ENSP00000500345.1; ENSG00000288257.1. [Q9BX79-1]
DR Ensembl; ENST00000672584.1; ENSP00000499915.1; ENSG00000288257.1. [Q9BX79-1]
DR Ensembl; ENST00000672836.1; ENSP00000500033.1; ENSG00000288257.1. [Q9BX79-5]
DR Ensembl; ENST00000673026.1; ENSP00000499878.1; ENSG00000288257.1. [Q9BX79-1]
DR Ensembl; ENST00000673039.1; ENSP00000500335.1; ENSG00000288257.1. [Q9BX79-6]
DR Ensembl; ENST00000673241.1; ENSP00000499866.1; ENSG00000288257.1. [Q9BX79-4]
DR Ensembl; ENST00000673414.1; ENSP00000500241.1; ENSG00000288257.1. [Q9BX79-1]
DR Ensembl; ENST00000673519.1; ENSP00000500334.1; ENSG00000288257.1. [Q9BX79-2]
DR GeneID; 64220; -.
DR KEGG; hsa:64220; -.
DR MANE-Select; ENST00000395105.9; ENSP00000378537.4; NM_022369.4; NP_071764.3.
DR UCSC; uc002axj.5; human. [Q9BX79-1]
DR CTD; 64220; -.
DR DisGeNET; 64220; -.
DR GeneCards; STRA6; -.
DR HGNC; HGNC:30650; STRA6.
DR HPA; ENSG00000137868; Tissue enhanced (cervix, placenta).
DR MalaCards; STRA6; -.
DR MIM; 601186; phenotype.
DR MIM; 610745; gene.
DR neXtProt; NX_Q9BX79; -.
DR OpenTargets; ENSG00000137868; -.
DR Orphanet; 98938; Colobomatous microphthalmia.
DR Orphanet; 2470; Matthew-Wood syndrome.
DR PharmGKB; PA134956551; -.
DR VEuPathDB; HostDB:ENSG00000137868; -.
DR eggNOG; ENOG502QRSS; Eukaryota.
DR GeneTree; ENSGT00940000153246; -.
DR HOGENOM; CLU_1639302_0_0_1; -.
DR InParanoid; Q9BX79; -.
DR OrthoDB; 325169at2759; -.
DR PhylomeDB; Q9BX79; -.
DR TreeFam; TF331851; -.
DR PathwayCommons; Q9BX79; -.
DR Reactome; R-HSA-2453864; Retinoid cycle disease events.
DR Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision).
DR SignaLink; Q9BX79; -.
DR SIGNOR; Q9BX79; -.
DR BioGRID-ORCS; 64220; 11 hits in 1067 CRISPR screens.
DR ChiTaRS; STRA6; human.
DR GenomeRNAi; 64220; -.
DR Pharos; Q9BX79; Tbio.
DR PRO; PR:Q9BX79; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9BX79; protein.
DR Bgee; ENSG00000137868; Expressed in stromal cell of endometrium and 94 other tissues.
DR ExpressionAtlas; Q9BX79; baseline and differential.
DR Genevisible; Q9BX79; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:LIFEdb.
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; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0030325; P:adrenal gland development; IMP:DFLAT.
DR GO; GO:0061143; P:alveolar primary septum development; IMP:DFLAT.
DR GO; GO:0048844; P:artery morphogenesis; IMP:DFLAT.
DR GO; GO:0001568; P:blood vessel development; IMP:DFLAT.
DR GO; GO:0043010; P:camera-type eye development; IMP:UniProtKB.
DR GO; GO:0050890; P:cognition; IMP:DFLAT.
DR GO; GO:0048589; P:developmental growth; IMP:DFLAT.
DR GO; GO:0060539; P:diaphragm development; IMP:DFLAT.
DR GO; GO:0048546; P:digestive tract morphogenesis; IMP:DFLAT.
DR GO; GO:0097070; P:ductus arteriosus closure; IMP:DFLAT.
DR GO; GO:0043583; P:ear development; IMP:DFLAT.
DR GO; GO:0060900; P:embryonic camera-type eye formation; IMP:DFLAT.
DR GO; GO:0048566; P:embryonic digestive tract development; IMP:DFLAT.
DR GO; GO:0061029; P:eyelid development in camera-type eye; IMP:DFLAT.
DR GO; GO:0060325; P:face morphogenesis; IMP:DFLAT.
DR GO; GO:0007631; P:feeding behavior; IMP:DFLAT.
DR GO; GO:0030540; P:female genitalia development; IMP:DFLAT.
DR GO; GO:0060322; P:head development; IMP:DFLAT.
DR GO; GO:0060323; P:head morphogenesis; IMP:DFLAT.
DR GO; GO:0007507; P:heart development; IMP:DFLAT.
DR GO; GO:0001822; P:kidney development; IMP:DFLAT.
DR GO; GO:0007612; P:learning; IMP:DFLAT.
DR GO; GO:0048286; P:lung alveolus development; IMP:DFLAT.
DR GO; GO:0030324; P:lung development; IMP:DFLAT.
DR GO; GO:0060426; P:lung vasculature development; IMP:DFLAT.
DR GO; GO:0050905; P:neuromuscular process; IMP:DFLAT.
DR GO; GO:0043585; P:nose morphogenesis; IMP:DFLAT.
DR GO; GO:0061205; P:paramesonephric duct development; IMP:DFLAT.
DR GO; GO:0048520; P:positive regulation of behavior; IMP:DFLAT.
DR GO; GO:0061156; P:pulmonary artery morphogenesis; IMP:DFLAT.
DR GO; GO:0003184; P:pulmonary valve morphogenesis; IMP:DFLAT.
DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR GO; GO:0034633; P:retinol transport; IDA:UniProtKB.
DR GO; GO:0048745; P:smooth muscle tissue development; IMP:DFLAT.
DR GO; GO:0061038; P:uterus morphogenesis; IMP:DFLAT.
DR GO; GO:0003281; P:ventricular septum development; IMP:DFLAT.
DR GO; GO:0071939; P:vitamin A import into cell; IBA:GO_Central.
DR GO; GO:0042297; P:vocal learning; IMP:DFLAT.
DR InterPro; IPR026612; STRA6.
DR PANTHER; PTHR21444:SF16; PTHR21444:SF16; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disease variant; Glycoprotein;
KW Membrane; Microphthalmia; Phosphoprotein; Receptor; Reference proteome;
KW Retinol-binding; Transmembrane; Transmembrane helix; Transport; Vitamin A.
FT CHAIN 1..667
FT /note="Receptor for retinol uptake STRA6"
FT /id="PRO_0000311228"
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..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 122..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..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..293
FT /note="Interaction with RBP1"
FT /evidence="ECO:0000269|PubMed:22665496"
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:0000269|PubMed:21368206"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1
FT /note="M -> MGGKGGGDTRGPVLFPCQLAQALSPRRAFPRELKEKGQRM (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_029437"
FT VAR_SEQ 1
FT /note="M -> MQIRLLRAELVVPLWQFIRQWPPGSDGWGQMEEKGQRM (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046776"
FT VAR_SEQ 1
FT /note="M -> MDSQGDWAAQEKGQRM (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047497"
FT VAR_SEQ 89..97
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11358845,
FT ECO:0000303|PubMed:12975309"
FT /id="VSP_029438"
FT VAR_SEQ 145..667
FT /note="AWKILGLFYYAALYYPLAACATAGHTAAHLLGSTLSWAHLGVQVWQRAECPQ
FT VPKIYKYYSLLASLPLLLGLGFLSLWYPVQLVRSFSRRTGAGSKGLQSSYSEEYLRNLL
FT CRKKLGSSYHTSKHGFLSWARVCLRHCIYTPQPGFHLPLKLVLSATLTGTAIYQVALLL
FT LVGVVPTIQKVRAGVTTDVSYLLAGFGIVLSEDKQEVVELVKHHLWALEVCYISALVLS
FT CLLTFLVLMRSLVTHRTNLRALHRGAALDLSPLHRSPHPSRQAIFCWMSFSAYQTAFIC
FT LGLLVQQIIFFLGTTALAFLVLMPVLHGRNLLLFRSLESSWPFWLTLALAVILQNMAAH
FT WVFLETHDGHPQLTNRRVLYAATFLLFPLNVLVGAMVATWRVLLSALYNAIHLGQMDLS
FT LLPPRAATLDPGYYTYRNFLKIEVSQSHPAMTAFCSLLLQAQSLLPRTMAAPQDSLRPG
FT EEDEGMQLLQTKDSMAKGARPGASRGRARWGLAYTLLHNPTLQVFRKTALLGANGAQP
FT -> NLPKITELRLVRAWI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029439"
FT VARIANT 90
FT /note="P -> L (in MCOPS9; dbSNP:rs118203961)"
FT /evidence="ECO:0000269|PubMed:17273977"
FT /id="VAR_037168"
FT VARIANT 217
FT /note="G -> E (in anophthalmia/microphthalmia;
FT dbSNP:rs909629751)"
FT /evidence="ECO:0000269|PubMed:19112531"
FT /id="VAR_060203"
FT VARIANT 293
FT /note="P -> L (in MCOPS9; dbSNP:rs118203958)"
FT /evidence="ECO:0000269|PubMed:17273977"
FT /id="VAR_037169"
FT VARIANT 304
FT /note="G -> K (in MCOPS9; also found in a family with
FT isolated colobomatous microphthalmia; affects STRA6 cell
FT surface expression and retinol uptake; requires 2
FT nucleotide substitutions; dbSNP:rs151341424)"
FT /evidence="ECO:0000269|PubMed:21901792"
FT /id="VAR_066849"
FT VARIANT 321
FT /note="T -> P (in MCOPS9; dbSNP:rs118203962)"
FT /evidence="ECO:0000269|PubMed:17273977"
FT /id="VAR_037170"
FT VARIANT 339
FT /note="G -> S (in dbSNP:rs17852249)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15498874"
FT /id="VAR_037171"
FT VARIANT 438
FT /note="Q -> R (in anophthalmia/microphthalmia;
FT dbSNP:rs869025269)"
FT /evidence="ECO:0000269|PubMed:19309693"
FT /id="VAR_060204"
FT VARIANT 517
FT /note="L -> F (in dbSNP:rs11545567)"
FT /id="VAR_037172"
FT VARIANT 527
FT /note="M -> I (in dbSNP:rs736118)"
FT /evidence="ECO:0000269|PubMed:11358845,
FT ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:14702039"
FT /id="VAR_037173"
FT VARIANT 638
FT /note="R -> P (in anophthalmia/microphthalmia;
FT dbSNP:rs144691445)"
FT /evidence="ECO:0000269|PubMed:19309693"
FT /id="VAR_060205"
FT VARIANT 644
FT /note="T -> M (in MCOPS9; loss of tyrosine phosphorylation;
FT dbSNP:rs118203960)"
FT /evidence="ECO:0000269|PubMed:17273977,
FT ECO:0000269|PubMed:21368206"
FT /id="VAR_037174"
FT VARIANT 655
FT /note="R -> C (in MCOPS9; dbSNP:rs118203959)"
FT /evidence="ECO:0000269|PubMed:17273977"
FT /id="VAR_037175"
FT MUTAGEN 255
FT /note="L->A: Loss of interaction with RBP1."
FT /evidence="ECO:0000269|PubMed:22665496"
FT MUTAGEN 643
FT /note="Y->F: Loss of tyrosine phosphorylation."
FT /evidence="ECO:0000269|PubMed:21368206"
FT CONFLICT 95
FT /note="A -> V (in Ref. 4; BAH12965)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="R -> Q (in Ref. 3; CAD97655)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="I -> M (in Ref. 4; BAH12965)"
FT /evidence="ECO:0000305"
FT CONFLICT 635
FT /note="G -> S (in Ref. 4; BAH13848)"
FT /evidence="ECO:0000305"
SQ 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
