S6A14_MOUSE
ID S6A14_MOUSE Reviewed; 638 AA.
AC Q9JMA9; Q91Y60; Q9D317; Q9R183;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Sodium- and chloride-dependent neutral and basic amino acid transporter B(0+) {ECO:0000305};
DE AltName: Full=Amino acid transporter ATB0+;
DE AltName: Full=Colonic system B0+ amino acid transporter CATB0+;
DE AltName: Full=Solute carrier family 6 member 14;
GN Name=Slc6a14 {ECO:0000312|MGI:MGI:1890216};
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, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND TRANSPORTER ACTIVITY.
RC STRAIN=ddY;
RX PubMed=11447016; DOI=10.1152/ajpgi.2001.281.2.g365;
RA Ugawa S., Sunouchi Y., Ueda T., Takahashi E., Saishin Y., Shimada S.;
RT "Characterization of a mouse colonic system B(0+) amino acid transporter
RT related to amino acid absorption in colon.";
RL Am. J. Physiol. 281:G365-G370(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND TRANSPORTER
RP ACTIVITY.
RC STRAIN=C57BL/6J; TISSUE=Colon;
RX PubMed=11306607; DOI=10.1172/jci12060;
RA Hatanaka T., Nakanishi T., Huang W., Leibach F.H., Prasad P.D.,
RA Ganapathy V., Ganapathy M.E.;
RT "Na(+)- and Cl(-)-coupled active transport of nitric oxide synthase
RT inhibitors via amino acid transport system B(0,+).";
RL J. Clin. Invest. 107:1035-1043(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Lung;
RA Revell L., Sloan J.L., Mager S.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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 [6]
RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11306651; DOI=10.1111/j.1469-7793.2001.0297f.x;
RA Nakanishi T., Hatanaka T., Huang W., Prasad P.D., Leibach F.H.,
RA Ganapathy M.E., Ganapathy V.;
RT "Na+- and Cl--coupled active transport of carnitine by the amino acid
RT transporter ATB(0,+) from mouse colon expressed in HRPE cells and Xenopus
RT oocytes.";
RL J. Physiol. (Lond.) 532:297-304(2001).
CC -!- FUNCTION: Amino acid transporter that plays an important role in the
CC absorption of amino acids in the intestinal tract. Mediates the uptake
CC of a broad range of neutral and cationic amino acids (with the
CC exception of proline) in a Na(+)/Cl(-)-dependent manner
CC (PubMed:11306607, PubMed:11447016). Transports non-alpha-amino acids
CC such as beta-alanine with low affinity, and has a higher affinity for
CC dipolar and cationic amino acids such as leucine and lysine (By
CC similarity). Can also transport carnitine and propionylcarnitine
CC coupled to the transmembrane gradients of Na(+) and Cl(-)
CC (PubMed:11306651). {ECO:0000250|UniProtKB:Q9UN76,
CC ECO:0000269|PubMed:11306607, ECO:0000269|PubMed:11306651,
CC ECO:0000269|PubMed:11447016}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + glycine(out) + 2 Na(+)(out) = chloride(in) +
CC glycine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:70691, ChEBI:CHEBI:17996,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57305;
CC Evidence={ECO:0000269|PubMed:11306607, ECO:0000269|PubMed:11447016};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + L-leucine(out) + 2 Na(+)(out) = chloride(in) +
CC L-leucine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71279, ChEBI:CHEBI:17996,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57427;
CC Evidence={ECO:0000250|UniProtKB:Q9UN76};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + L-glutamine(out) + 2 Na(+)(out) = chloride(in)
CC + L-glutamine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71283,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000250|UniProtKB:Q9UN76};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + L-arginine(out) + 2 Na(+)(out) = chloride(in)
CC + L-arginine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71287,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:32682;
CC Evidence={ECO:0000250|UniProtKB:Q9UN76};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine(out) + chloride(out) + 2 Na(+)(out) = (R)-
CC carnitine(in) + chloride(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71291,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:11306651};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + 2 Na(+)(out) + O-propanoyl-(R)-carnitine(out)
CC = chloride(in) + 2 Na(+)(in) + O-propanoyl-(R)-carnitine(in);
CC Xref=Rhea:RHEA:71295, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:53210; Evidence={ECO:0000269|PubMed:11306651};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + L-isoleucine(out) + 2 Na(+)(out) =
CC chloride(in) + L-isoleucine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71299,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:58045;
CC Evidence={ECO:0000250|UniProtKB:Q9UN76};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + L-methionine(out) + 2 Na(+)(out) =
CC chloride(in) + L-methionine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71303,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57844;
CC Evidence={ECO:0000250|UniProtKB:Q9UN76};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + L-valine(out) + 2 Na(+)(out) = chloride(in) +
CC L-valine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71307, ChEBI:CHEBI:17996,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57762;
CC Evidence={ECO:0000250|UniProtKB:Q9UN76};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + L-alanine(out) + 2 Na(+)(out) = chloride(in) +
CC L-alanine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71311, ChEBI:CHEBI:17996,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57972;
CC Evidence={ECO:0000250|UniProtKB:Q9UN76};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + L-serine(out) + 2 Na(+)(out) = chloride(in) +
CC L-serine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71315, ChEBI:CHEBI:17996,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:33384;
CC Evidence={ECO:0000250|UniProtKB:Q9UN76};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + L-cysteine(out) + 2 Na(+)(out) = chloride(in)
CC + L-cysteine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71319,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:35235;
CC Evidence={ECO:0000250|UniProtKB:Q9UN76};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + L-asparagine(out) + 2 Na(+)(out) =
CC chloride(in) + L-asparagine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71323,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:58048;
CC Evidence={ECO:0000250|UniProtKB:Q9UN76};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + L-threonine(out) + 2 Na(+)(out) = chloride(in)
CC + L-threonine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71327,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57926;
CC Evidence={ECO:0000250|UniProtKB:Q9UN76};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + L-phenylalanine(out) + 2 Na(+)(out) =
CC chloride(in) + L-phenylalanine(in) + 2 Na(+)(in);
CC Xref=Rhea:RHEA:71331, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:58095; Evidence={ECO:0000250|UniProtKB:Q9UN76};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + L-tryptophan(out) + 2 Na(+)(out) =
CC chloride(in) + L-tryptophan(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71335,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57912;
CC Evidence={ECO:0000250|UniProtKB:Q9UN76};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + L-tyrosine(out) + 2 Na(+)(out) = chloride(in)
CC + L-tyrosine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71339,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:58315;
CC Evidence={ECO:0000250|UniProtKB:Q9UN76};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + L-histidine(out) + 2 Na(+)(out) = chloride(in)
CC + L-histidine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71343,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57595;
CC Evidence={ECO:0000250|UniProtKB:Q9UN76};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + L-lysine(out) + 2 Na(+)(out) = chloride(in) +
CC L-lysine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71347, ChEBI:CHEBI:17996,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:32551;
CC Evidence={ECO:0000250|UniProtKB:Q9UN76};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:11306651}; Multi-
CC pass membrane protein {ECO:0000255}. Apical cell membrane
CC {ECO:0000269|PubMed:11447016}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the distal region of the intestinal
CC tract: cecum and colon. {ECO:0000269|PubMed:11306607,
CC ECO:0000269|PubMed:11447016}.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC 2.A.22) family. SLC6A14 subfamily. {ECO:0000305}.
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DR EMBL; AB033285; BAA94300.1; -; mRNA.
DR EMBL; AF320226; AAK43541.1; -; mRNA.
DR EMBL; AF161714; AAD49320.1; -; mRNA.
DR EMBL; AK018553; BAB31272.1; -; mRNA.
DR CCDS; CCDS30051.1; -.
DR RefSeq; NP_064433.3; NM_020049.4.
DR AlphaFoldDB; Q9JMA9; -.
DR SMR; Q9JMA9; -.
DR STRING; 10090.ENSMUSP00000033414; -.
DR GlyGen; Q9JMA9; 7 sites.
DR iPTMnet; Q9JMA9; -.
DR PhosphoSitePlus; Q9JMA9; -.
DR MaxQB; Q9JMA9; -.
DR PaxDb; Q9JMA9; -.
DR PRIDE; Q9JMA9; -.
DR ProteomicsDB; 253390; -.
DR DNASU; 56774; -.
DR Ensembl; ENSMUST00000033414; ENSMUSP00000033414; ENSMUSG00000031089.
DR GeneID; 56774; -.
DR KEGG; mmu:56774; -.
DR UCSC; uc009sur.2; mouse.
DR CTD; 11254; -.
DR MGI; MGI:1890216; Slc6a14.
DR VEuPathDB; HostDB:ENSMUSG00000031089; -.
DR eggNOG; KOG3660; Eukaryota.
DR GeneTree; ENSGT00940000159688; -.
DR HOGENOM; CLU_006855_4_1_1; -.
DR InParanoid; Q9JMA9; -.
DR OMA; KRMRVPI; -.
DR OrthoDB; 250396at2759; -.
DR PhylomeDB; Q9JMA9; -.
DR TreeFam; TF343812; -.
DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR Reactome; R-MMU-442660; Na+/Cl- dependent neurotransmitter transporters.
DR BioGRID-ORCS; 56774; 2 hits in 75 CRISPR screens.
DR PRO; PR:Q9JMA9; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9JMA9; protein.
DR Bgee; ENSMUSG00000031089; Expressed in left colon and 66 other tissues.
DR ExpressionAtlas; Q9JMA9; baseline and differential.
DR Genevisible; Q9JMA9; MM.
DR GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
DR GO; GO:0022858; F:alanine transmembrane transporter activity; ISO:MGI.
DR GO; GO:0005275; F:amine transmembrane transporter activity; ISS:MGI.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0032328; P:alanine transport; ISO:MGI.
DR GO; GO:0089718; P:amino acid import across plasma membrane; ISO:MGI.
DR GO; GO:0009636; P:response to toxic substance; ISO:MGI.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR000175; Na/ntran_symport.
DR InterPro; IPR037272; SNS_sf.
DR PANTHER; PTHR11616; PTHR11616; 1.
DR Pfam; PF00209; SNF; 1.
DR PRINTS; PR00176; NANEUSMPORT.
DR SUPFAM; SSF161070; SSF161070; 1.
DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..638
FT /note="Sodium- and chloride-dependent neutral and basic
FT amino acid transporter B(0+)"
FT /id="PRO_0000214796"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..230
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..496
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 559..579
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 580..638
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 618..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 90
FT /note="F -> V (in Ref. 3; AAD49320)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="L -> P (in Ref. 3; AAD49320)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="N -> S (in Ref. 2; AAK43541)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="W -> C (in Ref. 3; AAD49320)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="S -> P (in Ref. 3; AAD49320)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="N -> K (in Ref. 3; AAD49320)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="R -> I (in Ref. 4; BAB31272)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 638 AA; 71456 MW; 5D5A78E2DF7E7612 CRC64;
MDRLKCPNFF KCRQKEKVTA SSENFHVGEN DENQERGNWS KKSDYLLSMV GYAVGLGNVW
RFPYLTYTNG GGAFLIPYAI MLALAGLPLF FLECSLGQFA SLGPVSVWRI LPLFQGVGIT
MVLISVFVAI YYNVIIAYSL YYLFASFQSV LPWANCSSWA DENCSRTPIV TGCNVSIGAG
EMFMNISWVN TNNLTCLNGS EVFRPGQLPS EQYWDKVTLQ RSSGMDETGV VVWYLALCLL
LAWLIVGAAL FKGIKSSGKV VYFTALFPYV VLLILLIRGA TLEGASKGIS YYIGAQSNFT
KLREAEVWKD AATQIFYSLS VAWGGLVALS SYNKFNNNCY SDAIIVCLTN CLTSVFAGFA
IFSILGHMAH ISGKEVSQVV KSGFDLAFIA YPEALAQLPA GPFWSILFFF MLLTLGLDSQ
FASIETITTT FQDLFPKAMK RMRVPITLGC CLILFLLGLL CVTQAGIYWV HLIDHFCAGW
GILIAAILEI AGIIWIYGGN RFIEDIEMMI GAKRWIFWLW WRACWFVITP ILLSAILVWS
LVKFHRPDYA DIPYPDWGVA LGWCMIIFCI IWIPIMAIIK IVQAEGNILQ RIISCCRPAS
NWGPYLEKHR GERYRDMAEP AKETDHEIPT ISGSTKPE
