S38A5_HUMAN
ID S38A5_HUMAN Reviewed; 472 AA.
AC Q8WUX1; B3KT20; B5MDE6; B7WPJ9; Q6PIW9; Q8WYU2; Q96PQ4;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Sodium-coupled neutral amino acid transporter 5;
DE AltName: Full=Solute carrier family 38 member 5;
DE AltName: Full=System N transporter 2;
GN Name=SLC38A5; Synonyms=JM24, SN2, SNAT5; ORFNames=PP7194;
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] (ISOFORM 1), VARIANT THR-451, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RC TISSUE=Hepatoma;
RX PubMed=11243884; DOI=10.1006/bbrc.2001.4504;
RA Nakanishi T., Sugawara M., Huang W., Martindale R.G., Leibach F.H.,
RA Ganapathy M.E., Prasad P.D., Ganapathy V.;
RT "Structure, function, and tissue expression pattern of human SN2, a subtype
RT of the amino acid transport system N.";
RL Biochem. Biophys. Res. Commun. 281:1343-1348(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Functions as a sodium-dependent amino acid transporter which
CC countertransport protons. Mediates the saturable, pH-sensitive, and
CC electrogenic cotransport of several neutral amino acids including
CC glycine, asparagine, alanine, serine, glutamine and histidine with
CC sodium. {ECO:0000269|PubMed:11243884}.
CC -!- ACTIVITY REGULATION: Not inhibited by lithium.
CC {ECO:0000269|PubMed:11243884}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 mM for histidine (at pH 8.0) {ECO:0000269|PubMed:11243884};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WUX1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WUX1-2; Sequence=VSP_029702;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in stomach, brain, liver,
CC lung and intestinal tract. {ECO:0000269|PubMed:11243884}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL55865.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF276889; AAK61856.1; -; mRNA.
DR EMBL; AF318358; AAL55865.1; ALT_FRAME; mRNA.
DR EMBL; AK094788; BAG52932.1; -; mRNA.
DR EMBL; CH471224; EAW50785.1; -; Genomic_DNA.
DR EMBL; AF196972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019246; AAH19246.1; -; mRNA.
DR EMBL; BC027721; AAH27721.1; -; mRNA.
DR CCDS; CCDS14293.1; -. [Q8WUX1-1]
DR PIR; JC7626; JC7626.
DR RefSeq; NP_277053.2; NM_033518.3. [Q8WUX1-1]
DR RefSeq; XP_016885450.1; XM_017029961.1. [Q8WUX1-1]
DR AlphaFoldDB; Q8WUX1; -.
DR SMR; Q8WUX1; -.
DR BioGRID; 124974; 47.
DR IntAct; Q8WUX1; 9.
DR MINT; Q8WUX1; -.
DR STRING; 9606.ENSP00000471683; -.
DR TCDB; 2.A.18.6.15; the amino acid/auxin permease (aaap) family.
DR GlyGen; Q8WUX1; 1 site.
DR iPTMnet; Q8WUX1; -.
DR PhosphoSitePlus; Q8WUX1; -.
DR SwissPalm; Q8WUX1; -.
DR BioMuta; SLC38A5; -.
DR DMDM; 74730778; -.
DR EPD; Q8WUX1; -.
DR jPOST; Q8WUX1; -.
DR MassIVE; Q8WUX1; -.
DR MaxQB; Q8WUX1; -.
DR PaxDb; Q8WUX1; -.
DR PeptideAtlas; Q8WUX1; -.
DR PRIDE; Q8WUX1; -.
DR ProteomicsDB; 74716; -. [Q8WUX1-1]
DR ProteomicsDB; 74717; -. [Q8WUX1-2]
DR Antibodypedia; 43079; 103 antibodies from 17 providers.
DR DNASU; 92745; -.
DR Ensembl; ENST00000595796.5; ENSP00000471683.1; ENSG00000017483.16. [Q8WUX1-1]
DR Ensembl; ENST00000619100.4; ENSP00000478807.1; ENSG00000017483.16. [Q8WUX1-2]
DR Ensembl; ENST00000620913.5; ENSP00000481291.1; ENSG00000017483.16. [Q8WUX1-1]
DR GeneID; 92745; -.
DR KEGG; hsa:92745; -.
DR MANE-Select; ENST00000620913.5; ENSP00000481291.1; NM_033518.4; NP_277053.2.
DR UCSC; uc033ecl.2; human. [Q8WUX1-1]
DR CTD; 92745; -.
DR DisGeNET; 92745; -.
DR GeneCards; SLC38A5; -.
DR HGNC; HGNC:18070; SLC38A5.
DR HPA; ENSG00000017483; Tissue enriched (pancreas).
DR MIM; 300649; gene.
DR neXtProt; NX_Q8WUX1; -.
DR OpenTargets; ENSG00000017483; -.
DR PharmGKB; PA38289; -.
DR VEuPathDB; HostDB:ENSG00000017483; -.
DR eggNOG; KOG1305; Eukaryota.
DR GeneTree; ENSGT00940000161233; -.
DR HOGENOM; CLU_009020_0_2_1; -.
DR InParanoid; Q8WUX1; -.
DR OMA; DSQMAYT; -.
DR OrthoDB; 697331at2759; -.
DR PhylomeDB; Q8WUX1; -.
DR TreeFam; TF328787; -.
DR PathwayCommons; Q8WUX1; -.
DR Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
DR SignaLink; Q8WUX1; -.
DR BioGRID-ORCS; 92745; 18 hits in 703 CRISPR screens.
DR ChiTaRS; SLC38A5; human.
DR GenomeRNAi; 92745; -.
DR Pharos; Q8WUX1; Tbio.
DR PRO; PR:Q8WUX1; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8WUX1; protein.
DR Bgee; ENSG00000017483; Expressed in body of pancreas and 121 other tissues.
DR ExpressionAtlas; Q8WUX1; baseline and differential.
DR Genevisible; Q8WUX1; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0022858; F:alanine transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; TAS:Reactome.
DR GO; GO:0015187; F:glycine transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015182; F:L-asparagine transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0015186; F:L-glutamine transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0005290; F:L-histidine transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0015194; F:L-serine transmembrane transporter activity; ISS:ARUK-UCL.
DR GO; GO:0022889; F:serine transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0006865; P:amino acid transport; TAS:Reactome.
DR GO; GO:1903713; P:asparagine transmembrane transport; IMP:ARUK-UCL.
DR GO; GO:0006868; P:glutamine transport; IMP:ARUK-UCL.
DR GO; GO:0015816; P:glycine transport; IMP:ARUK-UCL.
DR GO; GO:1904557; P:L-alanine transmembrane transport; IMP:ARUK-UCL.
DR GO; GO:0089709; P:L-histidine transmembrane transport; IMP:ARUK-UCL.
DR GO; GO:0015825; P:L-serine transport; ISS:ARUK-UCL.
DR GO; GO:0032329; P:serine transport; IMP:ARUK-UCL.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..472
FT /note="Sodium-coupled neutral amino acid transporter 5"
FT /id="PRO_0000312115"
FT TOPO_DOM 1..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..87
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..166
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..334
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..399
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 421..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461..472
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 221..247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..51
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_029702"
FT VARIANT 451
FT /note="M -> T (in dbSNP:rs17281188)"
FT /evidence="ECO:0000269|PubMed:11243884"
FT /id="VAR_037396"
FT CONFLICT 456
FT /note="G -> S (in Ref. 1; AAK61856)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="G -> S (in Ref. 1; AAK61856)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 51457 MW; 2DDB4C03E5E78734 CRC64;
MELQDPKMNG ALPSDAVGYR QEREGFLPSR GPAPGSKPVQ FMDFEGKTSF GMSVFNLSNA
IMGSGILGLA YAMAHTGVIF FLALLLCIAL LSSYSIHLLL TCAGIAGIRA YEQLGQRAFG
PAGKVVVATV ICLHNVGAMS SYLFIIKSEL PLVIGTFLYM DPEGDWFLKG NLLIIIVSVL
IILPLALMKH LGYLGYTSGL SLTCMLFFLV SVIYKKFQLG CAIGHNETAM ESEALVGLPS
QGLNSSCEAQ MFTVDSQMSY TVPIMAFAFV CHPEVLPIYT ELCRPSKRRM QAVANVSIGA
MFCMYGLTAT FGYLTFYSSV KAEMLHMYSQ KDPLILCVRL AVLLAVTLTV PVVLFPIRRA
LQQLLFPGKA FSWPRHVAIA LILLVLVNVL VICVPTIRDI FGVIGSTSAP SLIFILPSIF
YLRIVPSEVE PFLSWPKIQA LCFGVLGVLF MAVSLGFMFA NWATGQSRMS GH
