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 24-JAN-2024, entry version 154. 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 a 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}; 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; 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 GlyCosmos; Q9BX79; 1 site, No reported glycans. 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; 9606-ENSP00000456609; -. DR PeptideAtlas; 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; 289 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 AGR; HGNC:30650; -. DR CTD; 64220; -. DR DisGeNET; 64220; -. DR GeneCards; STRA6; -. DR HGNC; HGNC:30650; STRA6. DR HPA; ENSG00000137868; Tissue enhanced (cervix). 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; 2962838at2759; -. 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; 13 hits in 1144 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 96 other cell types or tissues. DR ExpressionAtlas; Q9BX79; baseline and differential. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. 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: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-like. DR PANTHER; PTHR21444; COILED-COIL DOMAIN-CONTAINING PROTEIN 180; 1. DR PANTHER; PTHR21444:SF16; RECEPTOR FOR RETINOL UPTAKE STRA6; 1. DR Pfam; PF14752; RBP_receptor; 1. DR Genevisible; Q9BX79; HS. 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 //