STRA6_MOUSE
ID STRA6_MOUSE Reviewed; 670 AA.
AC O70491; Q6DIA8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Receptor for retinol uptake STRA6;
DE AltName: Full=Retinoic acid-responsive protein;
DE AltName: Full=Retinol-binding protein receptor STRA6;
DE AltName: Full=Stimulated by retinoic acid gene 6 protein {ECO:0000303|PubMed:9203140};
GN Name=Stra6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=9203140; DOI=10.1016/s0925-4773(97)00039-7;
RA Bouillet P., Sapin V., Chazaud C., Messaddeq N., Decimo D., Dolle P.,
RA Chambon P.;
RT "Developmental expression pattern of Stra6, a retinoic acid-responsive gene
RT encoding a new type of membrane protein.";
RL Mech. Dev. 63:173-186(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [3]
RP INDUCTION.
RX PubMed=7644503; DOI=10.1073/pnas.92.17.7854;
RA Taneja R., Bouillet P., Boylan J.F., Gaub M.-P., Roy B., Gudas L.J.,
RA Chambon P.;
RT "Reexpression of retinoic acid receptor (RAR) gamma or overexpression of
RT RAR alpha or RAR beta in RAR gamma-null F9 cells reveals a partial
RT functional redundancy between the three RAR types.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:7854-7858(1995).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=8792610;
RX DOI=10.1002/(sici)1520-6408(1996)19:1<66::aid-dvg7>3.0.co;2-z;
RA Chazaud C., Bouillet P., Oulad-Abdelghani M., Dolle P.;
RT "Restricted expression of a novel retinoic acid responsive gene during limb
RT bud dorsoventral patterning and endochondral ossification.";
RL Dev. Genet. 19:66-73(1996).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=10727869; DOI=10.1016/s0925-4773(00)00241-0;
RA Sapin V., Bouillet P., Oulad-Abdelghani M., Dastugue B., Chambon P.,
RA Dolle P.;
RT "Differential expression of retinoic acid-inducible (Stra) genes during
RT mouse placentation.";
RL Mech. Dev. 92:295-299(2000).
RN [6]
RP INDUCTION.
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 [7]
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 [8]
RP FUNCTION, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
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 [9]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=22467576; DOI=10.1167/iovs.11-8476;
RA Ruiz A., Mark M., Jacobs H., Klopfenstein M., Hu J., Lloyd M., Habib S.,
RA Tosha C., Radu R.A., Ghyselinck N.B., Nusinowitz S., Bok D.;
RT "Retinoid content, visual responses, and ocular morphology are compromised
RT in the retinas of mice lacking the retinol-binding protein receptor,
RT STRA6.";
RL Invest. Ophthalmol. Vis. Sci. 53:3027-3039(2012).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=23839944; DOI=10.1074/jbc.m113.484014;
RA Berry D.C., Jacobs H., Marwarha G., Gely-Pernot A., O'Byrne S.M.,
RA DeSantis D., Klopfenstein M., Feret B., Dennefeld C., Blaner W.S.,
RA Croniger C.M., Mark M., Noy N., Ghyselinck N.B.;
RT "The STRA6 receptor is essential for retinol-binding protein-induced
RT insulin resistance but not for maintaining vitamin A homeostasis in tissues
RT other than the eye.";
RL J. Biol. Chem. 288:24528-24539(2013).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=24852372; DOI=10.1093/hmg/ddu258;
RA Amengual J., Zhang N., Kemerer M., Maeda T., Palczewski K., Von Lintig J.;
RT "STRA6 is critical for cellular vitamin A uptake and homeostasis.";
RL Hum. Mol. Genet. 23:5402-5417(2014).
CC -!- FUNCTION: Functions as retinol transporter (PubMed:23839944,
CC PubMed:24852372). Accepts all-trans retinol from the extracellular
CC retinol-binding protein RBP4, facilitates retinol transport across the
CC cell membrane, and then transfers retinol to the cytoplasmic retinol-
CC binding protein RBP1. Retinol uptake is enhanced by LRAT, an enzyme
CC that converts retinol to all-trans retinyl esters, the storage forms of
CC vitamin A (By similarity). Contributes to the activation of a signaling
CC cascade that depends on retinol transport and LRAT-dependent generation
CC of retinol metabolites that then trigger activation of JAK2 and its
CC target STAT5, and ultimately increase the expression of SOCS3 and
CC inhibit cellular responses to insulin (PubMed:21368206,
CC PubMed:23839944). Important for the homeostasis of vitamin A and its
CC derivatives, such as retinoic acid and 11-cis-retinal (PubMed:22467576,
CC PubMed:24852372). STRA6-mediated transport is particularly important in
CC the eye, and under conditions of dietary vitamin A deficiency
CC (PubMed:22467576, PubMed:23839944, PubMed:24852372). Does not transport
CC retinoic acid (By similarity). {ECO:0000250|UniProtKB:Q9BX79,
CC ECO:0000269|PubMed:21368206, ECO:0000269|PubMed:22467576,
CC ECO:0000269|PubMed:23839944, ECO:0000269|PubMed:24852372}.
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:0000269|PubMed:9203140};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q0V8E7}. Note=In the
CC retinal pigment epithelium localizes to the basolateral membrane
CC (PubMed:22467576, PubMed:24852372). Plasma membrane of the basal pole
CC of Sertoli cells, absent in plasma membrane of neighboring
CC spermatogonia (PubMed:9203140). {ECO:0000250|UniProtKB:Q0V8E7,
CC ECO:0000269|PubMed:22467576, ECO:0000269|PubMed:9203140}.
CC -!- TISSUE SPECIFICITY: Widely expressed in the embryo (PubMed:9203140,
CC PubMed:23839944). Detected in adult in the retinal pigment epithelium
CC in the eye (PubMed:9203140, PubMed:22467576, PubMed:23839944,
CC PubMed:24852372). In the adult, is highly expressed in cells that
CC compose blood-organ barriers in the brain (choroid plexus and the brain
CC microvascular), in testis (the basal layer of the seminiferous
CC epithelium), in the yolk sac, and in the chorioallantoic placenta
CC (PubMed:9203140, PubMed:23839944). Detected in white adipose tissue and
CC skeletal muscle, but not in liver (at protein level) (PubMed:21368206).
CC Widely expressed in adult, with high expression levels in the eye
CC (PubMed:24852372). Detected in brain, cerebellum, testis, pituitary,
CC pancreas, kidney, spleen, and female genital tract; and at very low
CC levels in heart and lung (PubMed:9203140, PubMed:24852372). Not
CC detected in liver (PubMed:9203140). {ECO:0000269|PubMed:21368206,
CC ECO:0000269|PubMed:22467576, ECO:0000269|PubMed:23839944,
CC ECO:0000269|PubMed:24852372, ECO:0000269|PubMed:9203140}.
CC -!- DEVELOPMENTAL STAGE: During embryogenesis, strongly expressed in the
CC periocular mesenchyme, in the developing eyes, in respiratory
CC mesenchymes, and in respiratory and bronchial epithelium, as well as in
CC the developing central nervous system and in different embryonic gut
CC derivatives (the epithelium of the pharyngeal pouches, mesenchyme of
CC the esophagus, stomach, intestine, and rectum). In Sertoli cells
CC expression depends on the stage of the spermatogenic cycle. During
CC early placentation, is expressed in the yolk sac membrane and the
CC chorionic plate. Expression was no longer detected in the yolk sac
CC membrane during mid-late gestation, but was found in the labyrinthine
CC zone of the chorioallantoic placenta. Expressed during early
CC dorsoventral limb patterning and during endochondral ossification.
CC {ECO:0000269|PubMed:10727869, ECO:0000269|PubMed:8792610,
CC ECO:0000269|PubMed:9203140}.
CC -!- INDUCTION: By retinoic acid. Synergistically up-regulated by Wnt1 and
CC retinoids in mammary epithelial cells. {ECO:0000269|PubMed:11358845,
CC ECO:0000269|PubMed:11832495, ECO:0000269|PubMed:7644503,
CC ECO:0000269|PubMed:9203140}.
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). Phosphorylation requires the presence of LRAT,
CC suggesting it may be triggered by the uptake of retinol that is then
CC metabolized within the cell to retinoids that function as signaling
CC molecules (By similarity). {ECO:0000250|UniProtKB:Q9BX79,
CC ECO:0000269|PubMed:21368206}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype at birth (PubMed:22467576,
CC PubMed:23839944, PubMed:24852372). Measurement of the eye diameter
CC indicates a tendency towards slightly smaller eye diameter 6 weeks
CC after birth, and this difference persists in 5 and 10 month old animals
CC (PubMed:22467576). The retina inner and outer segments are shorter in
CC mutant mice (PubMed:22467576, PubMed:24852372). The number of cone
CC cells in the retina is reduced, giving rise to a reduced cone response
CC to light stimulation (PubMed:22467576). The retinal pigment epithelium
CC displays discolored regions, where cells have large vacuoles and a
CC reduced melanin content (PubMed:24852372). Retina and retinal pigment
CC epithelium from dark-adapted mutant mice display strongly reduced
CC levels of all-trans-retinol, all-trans-retinyl palmitate, 11-cis-
CC retinal, 11-cis-retinyl palmitate and all-trans-retinal
CC (PubMed:22467576, PubMed:24852372). Electroretinograms (ERG) of dark-
CC adapted retinas from mutant mice display reduced a- and b-wave
CC amplitude in response to light (PubMed:22467576). In another knockout
CC model, the electroretinogram shows a complete lack of response to light
CC (PubMed:24852372). Dietary vitamin A supplements can alleviate the
CC ocular retinoid deficiency, and can prevent the altered retinal
CC responses to light observed in mutant mice (PubMed:24852372). Other
CC tissues and organs (brain, heart, kidney, liver, lungs, muscle,
CC pancreas, spleen, testis and white adipose tissue) display grossly
CC normal retinoid levels in 12 week old mice kept on normal chow
CC (PubMed:23839944). Embryonic development appears grossly normal, also
CC when females are fed a vitamin A-deficient diet (PubMed:23839944).
CC Embryonic eye development is altered, leading to persistent
CC hyperplastic primary vitreous that forms a conical mass of cells
CC between the optic nerve exit point and the lens in the eyes of mutant
CC mice (PubMed:22467576). In contrast, persistent hyperplastic primary
CC vitreous was not observed in another knockout experiment
CC (PubMed:24852372). {ECO:0000269|PubMed:22467576,
CC ECO:0000269|PubMed:23839944, ECO:0000269|PubMed:24852372}.
CC -!- MISCELLANEOUS: The retinoic acid-induced activation is impaired in
CC retinoic acid receptor gamma-null F9 cells.
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DR EMBL; AF062476; AAC16016.1; -; mRNA.
DR EMBL; BC075657; AAH75657.1; -; mRNA.
DR CCDS; CCDS23236.1; -.
DR RefSeq; NP_001155947.1; NM_001162475.1.
DR RefSeq; NP_001155948.1; NM_001162476.1.
DR RefSeq; NP_001155951.1; NM_001162479.1.
DR RefSeq; NP_033317.2; NM_009291.2.
DR RefSeq; XP_006511004.2; XM_006510941.3.
DR RefSeq; XP_006511006.1; XM_006510943.3.
DR RefSeq; XP_006511007.1; XM_006510944.3.
DR RefSeq; XP_006511008.1; XM_006510945.3.
DR RefSeq; XP_006511009.1; XM_006510946.3.
DR AlphaFoldDB; O70491; -.
DR SMR; O70491; -.
DR STRING; 10090.ENSMUSP00000034880; -.
DR TCDB; 2.A.90.1.2; the vitamin a receptor/transporter (stra6) family.
DR GlyGen; O70491; 2 sites.
DR iPTMnet; O70491; -.
DR PhosphoSitePlus; O70491; -.
DR MaxQB; O70491; -.
DR PaxDb; O70491; -.
DR PeptideAtlas; O70491; -.
DR PRIDE; O70491; -.
DR ProteomicsDB; 258664; -.
DR DNASU; 20897; -.
DR GeneID; 20897; -.
DR KEGG; mmu:20897; -.
DR UCSC; uc009pwi.2; mouse.
DR CTD; 64220; -.
DR MGI; MGI:107742; Stra6.
DR eggNOG; ENOG502QRSS; Eukaryota.
DR InParanoid; O70491; -.
DR OrthoDB; 325169at2759; -.
DR PhylomeDB; O70491; -.
DR TreeFam; TF331851; -.
DR Reactome; R-MMU-2453902; The canonical retinoid cycle in rods (twilight vision).
DR BioGRID-ORCS; 20897; 7 hits in 73 CRISPR screens.
DR ChiTaRS; Stra6; mouse.
DR PRO; PR:O70491; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O70491; protein.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR GO; GO:0034632; F:retinol transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0030325; P:adrenal gland development; ISO:MGI.
DR GO; GO:0061143; P:alveolar primary septum development; ISO:MGI.
DR GO; GO:0048844; P:artery morphogenesis; ISO:MGI.
DR GO; GO:0001568; P:blood vessel development; ISO:MGI.
DR GO; GO:0043010; P:camera-type eye development; ISS:UniProtKB.
DR GO; GO:0050890; P:cognition; ISO:MGI.
DR GO; GO:0048589; P:developmental growth; ISO:MGI.
DR GO; GO:0060539; P:diaphragm development; ISO:MGI.
DR GO; GO:0048546; P:digestive tract morphogenesis; ISO:MGI.
DR GO; GO:0097070; P:ductus arteriosus closure; ISO:MGI.
DR GO; GO:0043583; P:ear development; ISO:MGI.
DR GO; GO:0060900; P:embryonic camera-type eye formation; ISO:MGI.
DR GO; GO:0048566; P:embryonic digestive tract development; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0061029; P:eyelid development in camera-type eye; ISO:MGI.
DR GO; GO:0060325; P:face morphogenesis; ISO:MGI.
DR GO; GO:0007631; P:feeding behavior; ISO:MGI.
DR GO; GO:0030540; P:female genitalia development; ISO:MGI.
DR GO; GO:0060322; P:head development; ISO:MGI.
DR GO; GO:0060323; P:head morphogenesis; ISO:MGI.
DR GO; GO:0007507; P:heart development; ISO:MGI.
DR GO; GO:0001822; P:kidney development; ISO:MGI.
DR GO; GO:0007612; P:learning; ISO:MGI.
DR GO; GO:0048286; P:lung alveolus development; ISO:MGI.
DR GO; GO:0030324; P:lung development; ISO:MGI.
DR GO; GO:0060426; P:lung vasculature development; ISO:MGI.
DR GO; GO:0050905; P:neuromuscular process; ISO:MGI.
DR GO; GO:0043585; P:nose morphogenesis; ISO:MGI.
DR GO; GO:0061205; P:paramesonephric duct development; ISO:MGI.
DR GO; GO:0048520; P:positive regulation of behavior; ISO:MGI.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IMP:MGI.
DR GO; GO:0061156; P:pulmonary artery morphogenesis; ISO:MGI.
DR GO; GO:0003184; P:pulmonary valve morphogenesis; ISO:MGI.
DR GO; GO:0034633; P:retinol transport; IMP:MGI.
DR GO; GO:0048745; P:smooth muscle tissue development; ISO:MGI.
DR GO; GO:0061038; P:uterus morphogenesis; ISO:MGI.
DR GO; GO:0003281; P:ventricular septum development; ISO:MGI.
DR GO; GO:0071939; P:vitamin A import into cell; IBA:GO_Central.
DR GO; GO:0042297; P:vocal learning; ISO:MGI.
DR InterPro; IPR026612; STRA6.
DR PANTHER; PTHR21444:SF16; PTHR21444:SF16; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Retinol-binding; Transmembrane; Transmembrane helix;
KW Transport; Vitamin A.
FT CHAIN 1..670
FT /note="Receptor for retinol uptake STRA6"
FT /id="PRO_0000311229"
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..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 119..144
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 166..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 190..205
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 227..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 318..368
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 390..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 445..474
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 496..510
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT INTRAMEM 511..548
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT TOPO_DOM 549..670
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1RAX4"
FT REGION 235..294
FT /note="Interaction with RBP1"
FT /evidence="ECO:0000250|UniProtKB:Q9BX79"
FT MOD_RES 644
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9BX79"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 234
FT /note="R -> P (in Ref. 2; AAH75657)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 670 AA; 73775 MW; 6ACE69F3EE16A4F7 CRC64;
MESQASENGS QTSSGVTDDY SSWYIEEPLG AEEVQPEGVI PLCQLTAPPA LLHACLASLS
FLVLLLLALL VRRRRLWPRC GHRGLGLPSP VDFLAGDLSW TVPAAVFVVL FSNLCLLLPD
ENPLPFLNLT AASSPDGEME TSRGPWKLLA LLYYPALYYP LAACASAGHQ AAFLLGTVLS
WAHFGVQVWQ KAECPQDPKI YKHYSLLASL PLLLGLGFLS LWYPVQLVQS LRHRTGAGSQ
GLQTSYSEKY LRTLLCPKKL DSCSHPASKR SLLSRAWAFS HHSIYTPQPG FRLPLKLVIS
ATLTGTATYQ VALLLLVSVV PTVQKVRAGI NTDVSYLLAG FGIVLSEDRQ EVVELVKHHL
WTVEACYISA LVLSCASTFL LLIRSLRTHR ANLQALHRGA ALDLDPPLQS IHPSRQAIVS
WMSFCAYQTA FSCLGLLVQQ VIFFLGTTSL AFLVFVPLLH GRNLLLLRSL ESTWPFWLTV
ALAVILQNIA ANWIFLRTHH GYPELTNRRM LCVATFLLFP INMLVGAIMA VWRVLISSLY
NTVHLGQMDL SLLPQRAASL DPGYHTYQNF LRIEASQSHP GVIAFCALLL HAPSPQPRPP
LAPQDSLRPA EEEEGMQLLQ TKDLMAKGAG HKGSQSRARW GLAYTLLHNP SLQAFRKAAL
TSAKANGTQP