GTR5_MOUSE
ID GTR5_MOUSE Reviewed; 501 AA.
AC Q9WV38; Q8R1N7;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 5 {ECO:0000305};
DE AltName: Full=Fructose transporter {ECO:0000305};
DE AltName: Full=Glucose transporter type 5, small intestine {ECO:0000303|PubMed:12031501};
DE Short=GLUT-5 {ECO:0000303|PubMed:12031501};
GN Name=Slc2a5 {ECO:0000312|MGI:MGI:1928369};
GN Synonyms=Glut5 {ECO:0000303|PubMed:12031501};
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INDUCTION BY FRUCTOSE, AND ACTIVITY REGULATION.
RC STRAIN=C57BL/6J;
RX PubMed=12031501; DOI=10.1016/s0167-4781(02)00284-1;
RA Kwon O., Levine M., Burant C.F.;
RT "Cloning and functional characterization of the mouse fructose transporter,
RT GLUT5.";
RL Biochim. Biophys. Acta 1576:191-197(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=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 GENOMIC DNA].
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 [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [6]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=18417103; DOI=10.1016/j.brainres.2008.02.094;
RA Wu X., Wang X., Gao J., Yu Y., Jia S., Zheng J., Dallos P., He D.Z.,
RA Cheatham M., Zuo J.;
RT "Glucose transporter 5 is undetectable in outer hair cells and does not
RT contribute to cochlear amplification.";
RL Brain Res. 1210:20-28(2008).
RN [7]
RP SUBCELLULAR LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=18496516; DOI=10.1038/ki.2008.184;
RA Singh A.K., Amlal H., Haas P.J., Dringenberg U., Fussell S., Barone S.L.,
RA Engelhardt R., Zuo J., Seidler U., Soleimani M.;
RT "Fructose-induced hypertension: essential role of chloride and fructose
RT absorbing transporters PAT1 and Glut5.";
RL Kidney Int. 74:438-447(2008).
RN [8]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INDUCTION BY FRUCTOSE.
RX PubMed=19091748; DOI=10.1074/jbc.m808128200;
RA Barone S., Fussell S.L., Singh A.K., Lucas F., Xu J., Kim C., Wu X., Yu Y.,
RA Amlal H., Seidler U., Zuo J., Soleimani M.;
RT "Slc2a5 (Glut5) is essential for the absorption of fructose in the
RT intestine and generation of fructose-induced hypertension.";
RL J. Biol. Chem. 284:5056-5066(2009).
RN [9]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INDUCTION BY FRUCTOSE.
RX PubMed=26071406; DOI=10.1096/fj.15-272195;
RA Patel C., Douard V., Yu S., Gao N., Ferraris R.P.;
RT "Transport, metabolism, and endosomal trafficking-dependent regulation of
RT intestinal fructose absorption.";
RL FASEB J. 29:4046-4058(2015).
CC -!- FUNCTION: Functions as a fructose transporter that has only low
CC activity with other monosaccharides (PubMed:12031501, PubMed:19091748).
CC Can mediate the uptake of deoxyglucose, but with low efficiency (By
CC similarity). Essential for fructose uptake in the small intestine
CC (PubMed:19091748, PubMed:26071406). Plays a role in the regulation of
CC salt uptake and blood pressure in response to dietary fructose
CC (PubMed:19091748). Required for the development of high blood pressure
CC in response to high dietary fructose intake (PubMed:19091748).
CC {ECO:0000250|UniProtKB:P43427, ECO:0000269|PubMed:12031501,
CC ECO:0000269|PubMed:19091748, ECO:0000269|PubMed:26071406}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose(out) = D-fructose(in); Xref=Rhea:RHEA:60372,
CC ChEBI:CHEBI:37721; Evidence={ECO:0000250|UniProtKB:P22732};
CC -!- ACTIVITY REGULATION: Fructose uptake is inhibited by cytochalasin B.
CC {ECO:0000269|PubMed:12031501}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:18496516, ECO:0000269|PubMed:19091748,
CC ECO:0000269|PubMed:26071406}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18496516}. Cell membrane
CC {ECO:0000269|PubMed:12031501, ECO:0000269|PubMed:19091748}; Multi-pass
CC membrane protein {ECO:0000305}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P43427}. Note=Localized on the apical membrane
CC of jejunum villi, but also on lateral plasma membranes of the villi
CC (PubMed:18496516, PubMed:26071406). Transport to the cell membrane is
CC dependent on RAB11A (PubMed:26071406). {ECO:0000269|PubMed:18496516,
CC ECO:0000269|PubMed:26071406}.
CC -!- TISSUE SPECIFICITY: Detected at the apical membrane of villi in the
CC jejunum (PubMed:18496516, PubMed:19091748, PubMed:26071406). Detected
CC in jejunum mucosa (PubMed:26071406). Detected in epididymis and whole
CC testis (at protein level) (PubMed:18417103). Detected in small
CC intestine, kidney and testis (PubMed:12031501, PubMed:18417103,
CC PubMed:19091748). Detected in cochlea, but not in inner or outer
CC cochlear hair cells (PubMed:18417103). {ECO:0000269|PubMed:12031501,
CC ECO:0000269|PubMed:18417103, ECO:0000269|PubMed:18496516,
CC ECO:0000269|PubMed:19091748}.
CC -!- INDUCTION: Up-regulated in jejunum by dietary fructose intake (at
CC protein level) (PubMed:18496516). Up-regulated in jejunum by dietary
CC fructose intake (PubMed:18496516, PubMed:26071406). Up-regulated by
CC dietary fructose intake in small intestine and testis
CC (PubMed:12031501). {ECO:0000269|PubMed:12031501,
CC ECO:0000269|PubMed:18496516}.
CC -!- DISRUPTION PHENOTYPE: Mice fed a standard diet appear normal and
CC healthy, and display no visible phenotype (PubMed:18417103,
CC PubMed:19091748, PubMed:26071406). Mutant mice show reduced food intake
CC when kept on a high-frucose diet and about 28% reduction of their body
CC weight within seven days. They loose more weight than wild-type mice
CC that receive similar amounts of high-fructose food (PubMed:19091748).
CC Mutant mice show strongly decreased fructose absorption in the jejunum
CC (PubMed:19091748, PubMed:26071406). Contrary to wild-type, mutant mice
CC have a strongly distended colon and caecum when kept on a high-fructose
CC diet. Their intestines look normal when they are fed a standard diet.
CC Contrary to wild-type, mutant mice do not display increased fructose
CC levels in blood serum when kept on a high-fructose diet. Contrary to
CC wild-type, they do not show increased salt absorption in response to
CC fructose, and do not develop high blood pressure in response to
CC fructose feeding. On the contrary, the blood pressure of mutant mice is
CC strongly decreased after five days on a high-fructose diet. Mutant mice
CC develop hypovolemic shock and die after 7 to 10 days on high-fructose
CC diet (PubMed:19091748). Mutant mice display no defects of cochlear
CC morphology or any hearing defects (PubMed:18417103).
CC {ECO:0000269|PubMed:18417103, ECO:0000269|PubMed:19091748,
CC ECO:0000269|PubMed:26071406}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
CC {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; AF161071; AAD42235.1; -; mRNA.
DR EMBL; AK029720; BAC26582.1; -; mRNA.
DR EMBL; AL606971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU210939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466594; EDL14883.1; -; Genomic_DNA.
DR EMBL; BC023500; AAH23500.1; -; mRNA.
DR CCDS; CCDS18968.1; -.
DR RefSeq; NP_062715.2; NM_019741.3.
DR RefSeq; XP_006539139.1; XM_006539076.3.
DR RefSeq; XP_017175818.1; XM_017320329.1.
DR AlphaFoldDB; Q9WV38; -.
DR SMR; Q9WV38; -.
DR BioGRID; 208011; 1.
DR STRING; 10090.ENSMUSP00000030826; -.
DR GlyGen; Q9WV38; 1 site.
DR iPTMnet; Q9WV38; -.
DR PhosphoSitePlus; Q9WV38; -.
DR jPOST; Q9WV38; -.
DR PaxDb; Q9WV38; -.
DR PRIDE; Q9WV38; -.
DR ProteomicsDB; 271187; -.
DR Antibodypedia; 1404; 446 antibodies from 33 providers.
DR DNASU; 56485; -.
DR Ensembl; ENSMUST00000030826; ENSMUSP00000030826; ENSMUSG00000028976.
DR GeneID; 56485; -.
DR KEGG; mmu:56485; -.
DR UCSC; uc008vxk.1; mouse.
DR CTD; 6518; -.
DR MGI; MGI:1928369; Slc2a5.
DR VEuPathDB; HostDB:ENSMUSG00000028976; -.
DR eggNOG; KOG0569; Eukaryota.
DR GeneTree; ENSGT00940000156846; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; Q9WV38; -.
DR OMA; VAQFLCM; -.
DR OrthoDB; 326501at2759; -.
DR PhylomeDB; Q9WV38; -.
DR TreeFam; TF313762; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8981373; Intestinal hexose absorption.
DR BioGRID-ORCS; 56485; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q9WV38; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9WV38; protein.
DR Bgee; ENSMUSG00000028976; Expressed in seminiferous tubule of testis and 89 other tissues.
DR Genevisible; Q9WV38; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
DR GO; GO:0070061; F:fructose binding; ISS:UniProtKB.
DR GO; GO:0005353; F:fructose transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0071332; P:cellular response to fructose stimulus; IDA:UniProtKB.
DR GO; GO:1990539; P:fructose import across plasma membrane; IMP:UniProtKB.
DR GO; GO:0015755; P:fructose transmembrane transport; ISO:MGI.
DR GO; GO:1904659; P:glucose transmembrane transport; ISO:MGI.
DR GO; GO:0015749; P:monosaccharide transmembrane transport; IBA:GO_Central.
DR GO; GO:0003044; P:regulation of systemic arterial blood pressure mediated by a chemical signal; IMP:UniProtKB.
DR GO; GO:0009750; P:response to fructose; IMP:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR002442; Fru_transpt_5.
DR InterPro; IPR045263; GLUT.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR PANTHER; PTHR23503; PTHR23503; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR01194; GLUCTRSPORT5.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Glycoprotein; Membrane; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..501
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 5"
FT /id="PRO_0000050370"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 18..38
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 39..67
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 68..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 91..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 98..118
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 119..125
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 126..148
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 149..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 161..181
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 182..191
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 192..212
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 213..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 277..297
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 298..312
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 313..333
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 334..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 342..362
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 363..370
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 371..393
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 394..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 412..432
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 433..438
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 439..459
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 460..501
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT BINDING 31
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT BINDING 166
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT BINDING 287
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT BINDING 295..297
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT BINDING 386
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT BINDING 418..419
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P22732"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 84
FT /note="G -> S (in Ref. 1; AAD42235)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="M -> V (in Ref. 1; AAD42235)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="T -> N (in Ref. 1; AAD42235)"
FT /evidence="ECO:0000305"
FT CONFLICT 97..99
FT /note="RKG -> KKR (in Ref. 1; AAD42235)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="L -> F (in Ref. 1; AAD42235)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="L -> I (in Ref. 1; AAD42235)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="N -> I (in Ref. 1; AAD42235)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 55409 MW; 4F562A3BF848E5C7 CRC64;
MEEKHQEETG ELTLVLALAT LIAAFGSSFQ YGYNVAAVNS PSEFMQQFYN DTYYDRNEEN
IESFTLTLLW SLTVSMFPFG GFIGSLMVGT LVNKLGRKGA LLFNNIFSIL PAILMGCSQI
AQSFELIIIS RLLVGICAGI SSNVVPMYLG ELAPKNLRGA LGVVPQLFIT VGILVAQLFG
LRSLLANEDG WPVLLGLTGV PAGLQLLLLP FFPESPRYLL IQKKDEAAAE RALQTLRGWK
DVHLEMEEIR KEDEAEKAAG FISVWKLFTM QSLRWQLISM IVLMAGQQLS GVNAIYYYAD
QIYLSAGVKS DDVQYVTAGT GAVNVFMTIL TIFVVELWGR RFLLLVGFST CLIACLVLTA
ALALQNTISW MPYISIVCVI VYVIGHALGP SPIPALLITE IFLQSSRPAA YMIGGSVHWL
SNFTVGLIFP FIQMGLGPYS FIIFATICFL TTIYIFMVVP ETKGRTFIEI NQIFTMKNKV
SDVYPKKEEE LGALPHAILE Q
