SCRB1_MOUSE
ID SCRB1_MOUSE Reviewed; 509 AA.
AC Q61009; D3Z2V4; Q3TZ42; Q4FK30; Q9CWJ7;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Scavenger receptor class B member 1;
DE Short=SRB1;
DE AltName: Full=SR-BI;
GN Name=Scarb1; Synonyms=Srb1;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=8560269; DOI=10.1126/science.271.5248.518;
RA Acton S., Rigotti A., Landschulz K.T., Xu S., Hobbs H.H., Krieger M.;
RT "Identification of scavenger receptor SR-BI as a high density lipoprotein
RT receptor.";
RL Science 271:518-520(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Dendritic cell, Embryo, Embryonic stem cell, Inner ear, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 463-509 (ISOFORMS 1 AND 2), FUNCTION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX PubMed=9254074;
RA Webb N.R., de Villiers W.J., Connell P.M., de Beer F.C.,
RA van der Westhuyzen D.R.;
RT "Alternative forms of the scavenger receptor BI (SR-BI).";
RL J. Lipid Res. 38:1490-1495(1997).
RN [8]
RP FUNCTION, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP PALMITOYLATION AT CYS-462, AND INDUCTION BY ACTH.
RX PubMed=9614139; DOI=10.1074/jbc.273.24.15241;
RA Webb N.R., Connell P.M., Graf G.A., Smart E.J., de Villiers W.J.,
RA de Beer F.C., van der Westhuyzen D.R.;
RT "SR-BII, an isoform of the scavenger receptor BI containing an alternate
RT cytoplasmic tail, mediates lipid transfer between high density lipoprotein
RT and cells.";
RL J. Biol. Chem. 273:15241-15248(1998).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP DISULFIDE BONDS.
RX PubMed=21675794; DOI=10.1021/bi2005625;
RA Papale G.A., Hanson P.J., Sahoo D.;
RT "Extracellular disulfide bonds support scavenger receptor class B type I-
RT mediated cholesterol transport.";
RL Biochemistry 50:6245-6254(2011).
CC -!- FUNCTION: Receptor for different ligands such as phospholipids,
CC cholesterol ester, lipoproteins, phosphatidylserine and apoptotic cells
CC (By similarity). Both isoform 1 and isoform 2 act as receptors for HDL,
CC mediating selective uptake of cholesteryl ether and HDL-dependent
CC cholesterol efflux (PubMed:9254074, PubMed:9614139). Also facilitates
CC the flux of free and esterified cholesterol between the cell surface
CC and apoB-containing lipoproteins and modified lipoproteins, although
CC less efficiently than HDL. May be involved in the phagocytosis of
CC apoptotic cells, via its phosphatidylserine binding activity (By
CC similarity). {ECO:0000250|UniProtKB:Q8WTV0, ECO:0000269|PubMed:9254074,
CC ECO:0000269|PubMed:9614139}.
CC -!- SUBUNIT: The C-terminal region binds to PDZK1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9254074,
CC ECO:0000269|PubMed:9614139}; Multi-pass membrane protein {ECO:0000250}.
CC Membrane, caveola {ECO:0000269|PubMed:9614139}; Multi-pass membrane
CC protein {ECO:0000250}. Note=Predominantly localized to cholesterol and
CC sphingomyelin-enriched domains within the plasma membrane, called
CC caveolae. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:9614139}. Membrane, caveola
CC {ECO:0000269|PubMed:9614139}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC {ECO:0000269|PubMed:9614139}. Membrane, caveola
CC {ECO:0000269|PubMed:9614139}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=SR-BI {ECO:0000303|PubMed:8560269}, SR-BI.1
CC {ECO:0000303|PubMed:9254074};
CC IsoId=Q61009-1; Sequence=Displayed;
CC Name=2; Synonyms=SR-BI.2 {ECO:0000303|PubMed:9254074}, SR-BII
CC {ECO:0000303|PubMed:9614139};
CC IsoId=Q61009-2; Sequence=VSP_058986;
CC -!- TISSUE SPECIFICITY: Expressed primarily in liver, ovary and adrenal
CC gland, and, at lower levels in other non-placental steroidogenic
CC tissues, including adipose tissue, mammary gland and testis (at protein
CC level) (PubMed:8560269, PubMed:9254074, PubMed:9614139). Isoform 2 is
CC expressed at lower levels than isoform 1 in liver, testis and adrenal
CC gland (PubMed:9614139). At the mRNA, but not at the protein level,
CC isoform 2 is the predominant isoform in testis (80%) (PubMed:9254074).
CC {ECO:0000269|PubMed:8560269, ECO:0000269|PubMed:9254074,
CC ECO:0000269|PubMed:9614139}.
CC -!- INDUCTION: Both isoform 1 and isoform 2 are up-regulated in response to
CC adrenocorticotropic hormone (ACTH). {ECO:0000305|PubMed:9614139}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: The six cysteines of the extracellular domain are all involved in
CC intramolecular disulfide bonds.
CC -!- SIMILARITY: Belongs to the CD36 family. {ECO:0000305}.
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DR EMBL; U37799; AAC52378.1; -; mRNA.
DR EMBL; AK010622; BAB27068.1; -; mRNA.
DR EMBL; AK028191; BAC25802.1; -; mRNA.
DR EMBL; AK033114; BAC28157.1; -; mRNA.
DR EMBL; AK154933; BAE32934.1; -; mRNA.
DR EMBL; AK158122; BAE34368.1; -; mRNA.
DR EMBL; AK169906; BAE41449.1; -; mRNA.
DR EMBL; AC162802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT010222; CAJ18430.1; -; mRNA.
DR EMBL; CH466529; EDL19562.1; -; Genomic_DNA.
DR EMBL; CH466529; EDL19563.1; -; Genomic_DNA.
DR EMBL; BC004656; AAH04656.1; -; mRNA.
DR CCDS; CCDS19683.1; -. [Q61009-1]
DR CCDS; CCDS57383.1; -. [Q61009-2]
DR RefSeq; NP_001192011.1; NM_001205082.1. [Q61009-2]
DR RefSeq; NP_058021.1; NM_016741.2. [Q61009-1]
DR PDB; 3R69; X-ray; 1.50 A; A/B=505-509.
DR PDB; 5KTF; NMR; -; A=405-475.
DR PDBsum; 3R69; -.
DR PDBsum; 5KTF; -.
DR AlphaFoldDB; Q61009; -.
DR SMR; Q61009; -.
DR STRING; 10090.ENSMUSP00000083242; -.
DR BindingDB; Q61009; -.
DR ChEMBL; CHEMBL1741203; -.
DR GlyGen; Q61009; 11 sites.
DR iPTMnet; Q61009; -.
DR PhosphoSitePlus; Q61009; -.
DR SwissPalm; Q61009; -.
DR EPD; Q61009; -.
DR jPOST; Q61009; -.
DR MaxQB; Q61009; -.
DR PaxDb; Q61009; -.
DR PRIDE; Q61009; -.
DR ProteomicsDB; 255369; -. [Q61009-1]
DR ProteomicsDB; 255370; -. [Q61009-2]
DR Antibodypedia; 31879; 646 antibodies from 40 providers.
DR DNASU; 20778; -.
DR Ensembl; ENSMUST00000086075; ENSMUSP00000083242; ENSMUSG00000037936. [Q61009-1]
DR Ensembl; ENSMUST00000111390; ENSMUSP00000107021; ENSMUSG00000037936. [Q61009-2]
DR GeneID; 20778; -.
DR KEGG; mmu:20778; -.
DR UCSC; uc008zrd.2; mouse. [Q61009-1]
DR UCSC; uc008zre.2; mouse.
DR CTD; 949; -.
DR MGI; MGI:893578; Scarb1.
DR VEuPathDB; HostDB:ENSMUSG00000037936; -.
DR eggNOG; KOG3776; Eukaryota.
DR GeneTree; ENSGT00940000153372; -.
DR HOGENOM; CLU_019853_4_0_1; -.
DR InParanoid; Q61009; -.
DR OMA; DENYWIN; -.
DR OrthoDB; 1106566at2759; -.
DR PhylomeDB; Q61009; -.
DR TreeFam; TF317925; -.
DR Reactome; R-MMU-3000471; Scavenging by Class B Receptors.
DR Reactome; R-MMU-8964011; HDL clearance.
DR BioGRID-ORCS; 20778; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Scarb1; mouse.
DR PRO; PR:Q61009; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q61009; protein.
DR Bgee; ENSMUSG00000037936; Expressed in adrenal gland and 265 other tissues.
DR ExpressionAtlas; Q61009; baseline and differential.
DR Genevisible; Q61009; MM.
DR GO; GO:0005901; C:caveola; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0031528; C:microvillus membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
DR GO; GO:0001540; F:amyloid-beta binding; IGI:ARUK-UCL.
DR GO; GO:0034186; F:apolipoprotein A-I binding; ISO:MGI.
DR GO; GO:0034185; F:apolipoprotein binding; IPI:BHF-UCL.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; IDA:BHF-UCL.
DR GO; GO:0070506; F:high-density lipoprotein particle receptor activity; ISS:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; IBA:GO_Central.
DR GO; GO:0001530; F:lipopolysaccharide binding; ISO:MGI.
DR GO; GO:0001875; F:lipopolysaccharide immune receptor activity; ISO:MGI.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; ISS:BHF-UCL.
DR GO; GO:0001786; F:phosphatidylserine binding; ISO:MGI.
DR GO; GO:0005044; F:scavenger receptor activity; IBA:GO_Central.
DR GO; GO:0044406; P:adhesion of symbiont to host; ISO:MGI.
DR GO; GO:0006702; P:androgen biosynthetic process; ISO:MGI.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; IMP:MGI.
DR GO; GO:0046867; P:carotenoid transport; IMP:MGI.
DR GO; GO:0006707; P:cholesterol catabolic process; IDA:MGI.
DR GO; GO:0033344; P:cholesterol efflux; IDA:BHF-UCL.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
DR GO; GO:0070508; P:cholesterol import; IDA:BHF-UCL.
DR GO; GO:0030301; P:cholesterol transport; IDA:MGI.
DR GO; GO:0032497; P:detection of lipopolysaccharide; ISO:MGI.
DR GO; GO:0001935; P:endothelial cell proliferation; IMP:MGI.
DR GO; GO:0034384; P:high-density lipoprotein particle clearance; ISS:BHF-UCL.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IMP:BHF-UCL.
DR GO; GO:0098856; P:intestinal lipid absorption; IMP:MGI.
DR GO; GO:0006869; P:lipid transport; ISO:MGI.
DR GO; GO:0015920; P:lipopolysaccharide transport; ISO:MGI.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; IMP:BHF-UCL.
DR GO; GO:0006910; P:phagocytosis, recognition; ISO:MGI.
DR GO; GO:0015914; P:phospholipid transport; IMP:BHF-UCL.
DR GO; GO:0034381; P:plasma lipoprotein particle clearance; IBA:GO_Central.
DR GO; GO:0010886; P:positive regulation of cholesterol storage; ISS:BHF-UCL.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; ISO:MGI.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0043654; P:recognition of apoptotic cell; ISS:BHF-UCL.
DR GO; GO:0050764; P:regulation of phagocytosis; ISO:MGI.
DR GO; GO:0010899; P:regulation of phosphatidylcholine catabolic process; IMP:BHF-UCL.
DR GO; GO:0043691; P:reverse cholesterol transport; IMP:BHF-UCL.
DR GO; GO:0070328; P:triglyceride homeostasis; IMP:BHF-UCL.
DR GO; GO:0035461; P:vitamin transmembrane transport; ISO:MGI.
DR InterPro; IPR005428; CD36/SCARB1/SNMP1.
DR InterPro; IPR002159; CD36_fam.
DR PANTHER; PTHR11923; PTHR11923; 1.
DR Pfam; PF01130; CD36; 1.
DR PRINTS; PR01610; CD36ANTIGEN.
DR PRINTS; PR01609; CD36FAMILY.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..509
FT /note="Scavenger receptor class B member 1"
FT /id="PRO_0000144161"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..440
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..509
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 462
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:9614139"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 251..384
FT /evidence="ECO:0000305|PubMed:21675794"
FT VAR_SEQ 468..509
FT /note="EKCFLFWSGSKKGSQDKEAIQAYSESLMSPAAKGTVLQEAKL -> GPEDTI
FT SPPNLIAWSDQPPSPYTPLLEDSLSGQPTSAMA (in isoform 2)"
FT /id="VSP_058986"
FT CONFLICT 235
FT /note="D -> G (in Ref. 2; BAE34368)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="S -> F (in Ref. 2; BAB27068)"
FT /evidence="ECO:0000305"
FT HELIX 407..417
FT /evidence="ECO:0007829|PDB:5KTF"
FT TURN 418..422
FT /evidence="ECO:0007829|PDB:5KTF"
FT HELIX 427..434
FT /evidence="ECO:0007829|PDB:5KTF"
FT HELIX 440..455
FT /evidence="ECO:0007829|PDB:5KTF"
FT HELIX 457..468
FT /evidence="ECO:0007829|PDB:5KTF"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:5KTF"
SQ SEQUENCE 509 AA; 56754 MW; 5CFCDD62DD6ECB1C CRC64;
MGGSSRARWV ALGLGALGLL FAALGVVMIL MVPSLIKQQV LKNVRIDPSS LSFGMWKEIP
VPFYLSVYFF EVVNPNEVLN GQKPVVRERG PYVYREFRQK VNITFNDNDT VSFVENRSLH
FQPDKSHGSE SDYIVLPNIL VLGGSILMES KPVSLKLMMT LALVTMGQRA FMNRTVGEIL
WGYDDPFVHF LNTYLPDMLP IKGKFGLFVG MNNSNSGVFT VFTGVQNFSR IHLVDKWNGL
SKIDYWHSEQ CNMINGTSGQ MWAPFMTPES SLEFFSPEAC RSMKLTYNES RVFEGIPTYR
FTAPDTLFAN GSVYPPNEGF CPCRESGIQN VSTCRFGAPL FLSHPHFYNA DPVLSEAVLG
LNPNPKEHSL FLDIHPVTGI PMNCSVKMQL SLYIKSVKGI GQTGKIEPVV LPLLWFEQSG
AMGGKPLSTF YTQLVLMPQV LHYAQYVLLG LGGLLLLVPI ICQLRSQEKC FLFWSGSKKG
SQDKEAIQAY SESLMSPAAK GTVLQEAKL
