CTR2_MOUSE
ID CTR2_MOUSE Reviewed; 657 AA.
AC P18581; E9QPL9; Q38RA6; Q3TB99; Q3U3R5;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Cationic amino acid transporter 2;
DE Short=CAT-2;
DE Short=CAT2;
DE AltName: Full=20.5;
DE AltName: Full=Low affinity cationic amino acid transporter 2 {ECO:0000303|PubMed:8385111};
DE AltName: Full=Solute carrier family 7 member 2;
DE AltName: Full=T-cell early activation protein {ECO:0000303|PubMed:8195186};
DE Short=TEA {ECO:0000303|PubMed:8195186};
GN Name=Slc7a2; Synonyms=Atrc2, Tea;
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 2).
RC STRAIN=AKR/J; TISSUE=T-cell;
RX PubMed=1694015; DOI=10.1128/mcb.10.7.3663-3674.1990;
RA Macleod C.L., Finley K., Kakuda D., Kozak C.A., Wilkinson M.F.;
RT "Activated T cells express a novel gene on chromosome 8 that is closely
RT related to the murine ecotropic retroviral receptor.";
RL Mol. Cell. Biol. 10:3663-3674(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND GLYCOSYLATION.
RC TISSUE=Liver;
RX PubMed=8385111; DOI=10.1016/s0021-9258(18)53209-9;
RA Closs E.I., Albritton L.M., Kim J.W., Cunningham J.M.;
RT "Identification of a low affinity, high capacity transporter of cationic
RT amino acids in mouse liver.";
RL J. Biol. Chem. 268:7538-7544(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP ALTERNATIVE SPLICING.
RC TISSUE=Liver;
RX PubMed=8195186; DOI=10.1016/s0021-9258(17)40699-5;
RA Kavanaugh M.P., Wang H., Zhang Z., Zhang W., Wu Y.N., Dechant E.,
RA North R.A., Kabat D.;
RT "Control of cationic amino acid transport and retroviral receptor functions
RT in a membrane protein family.";
RL J. Biol. Chem. 269:15445-15450(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=Swiss Webster / NIH;
RX PubMed=16239143; DOI=10.1016/j.cell.2005.08.033;
RA Prasanth K.V., Prasanth S.G., Xuan Z., Hearn S., Freier S.M., Bennett C.F.,
RA Zhang M.Q., Spector D.L.;
RT "Regulating gene expression through RNA nuclear retention.";
RL Cell 123:249-263(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, and NOD;
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=16670299; DOI=10.4049/jimmunol.176.10.5918;
RA Yeramian A., Martin L., Serrat N., Arpa L., Soler C., Bertran J.,
RA McLeod C., Palacin M., Modolell M., Lloberas J., Celada A.;
RT "Arginine transport via cationic amino acid transporter 2 plays a critical
RT regulatory role in classical or alternative activation of macrophages.";
RL J. Immunol. 176:5918-5924(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Isoform 1 functions as low-affinity, high capacity permease
CC involved in the transport of the cationic amino acids (arginine, lysine
CC and ornithine). Isoform 2 also functions as permease that mediates the
CC transport of the cationic amino acids (arginine, lysine and ornithine),
CC but it has much higher affinity for arginine than isoform 1. May play a
CC role in classical or alternative activation of macrophages via its role
CC in arginine transport. {ECO:0000269|PubMed:16670299,
CC ECO:0000269|PubMed:8195186, ECO:0000269|PubMed:8385111}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8195186,
CC ECO:0000269|PubMed:8385111}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:8195186, ECO:0000269|PubMed:8385111}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Alpha;
CC IsoId=P18581-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=P18581-2; Sequence=VSP_000025;
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level)
CC (PubMed:8385111). Highest expression in liver and T-cells. Also
CC expressed in brain and lung. {ECO:0000269|PubMed:16239143,
CC ECO:0000269|PubMed:8385111}.
CC -!- INDUCTION: By macrophage activation. {ECO:0000269|PubMed:16670299}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:8385111}.
CC -!- MISCELLANEOUS: [Isoform 2]: Affinity of isoform 2 for arginine uptake
CC is 70-fold higher than for isoform 1. {ECO:0000269|PubMed:8195186}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. Cationic amino acid transporter (CAT) (TC 2.A.3.3) family.
CC {ECO:0000305}.
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DR EMBL; M62838; AAA75250.1; -; mRNA.
DR EMBL; L03290; AAA37372.1; -; mRNA.
DR EMBL; L11600; AAA37350.1; -; mRNA.
DR EMBL; L29006; AAA20397.1; -; mRNA.
DR EMBL; DQ086834; AAY87029.1; -; mRNA.
DR EMBL; AK154621; BAE32720.1; -; mRNA.
DR EMBL; AK171369; BAE42415.1; -; mRNA.
DR EMBL; AC116511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC127082; AAI27083.1; -; mRNA.
DR CCDS; CCDS22258.1; -. [P18581-1]
DR CCDS; CCDS40327.1; -. [P18581-2]
DR PIR; A54011; A54011.
DR RefSeq; NP_001038205.1; NM_001044740.2. [P18581-2]
DR RefSeq; NP_031540.2; NM_007514.3. [P18581-1]
DR RefSeq; XP_006509316.1; XM_006509253.3. [P18581-2]
DR AlphaFoldDB; P18581; -.
DR SMR; P18581; -.
DR BioGRID; 198276; 10.
DR STRING; 10090.ENSMUSP00000096414; -.
DR TCDB; 2.A.3.3.2; the amino acid-polyamine-organocation (apc) family.
DR GlyGen; P18581; 3 sites.
DR iPTMnet; P18581; -.
DR PhosphoSitePlus; P18581; -.
DR SwissPalm; P18581; -.
DR jPOST; P18581; -.
DR MaxQB; P18581; -.
DR PaxDb; P18581; -.
DR PRIDE; P18581; -.
DR ProteomicsDB; 279199; -. [P18581-1]
DR ProteomicsDB; 279200; -. [P18581-2]
DR Antibodypedia; 2114; 120 antibodies from 24 providers.
DR DNASU; 11988; -.
DR Ensembl; ENSMUST00000057784; ENSMUSP00000058866; ENSMUSG00000031596. [P18581-1]
DR Ensembl; ENSMUST00000098816; ENSMUSP00000096414; ENSMUSG00000031596. [P18581-2]
DR Ensembl; ENSMUST00000117077; ENSMUSP00000113729; ENSMUSG00000031596. [P18581-2]
DR GeneID; 11988; -.
DR KEGG; mmu:11988; -.
DR UCSC; uc009lnf.1; mouse. [P18581-1]
DR UCSC; uc009lng.1; mouse. [P18581-2]
DR CTD; 6542; -.
DR MGI; MGI:99828; Slc7a2.
DR VEuPathDB; HostDB:ENSMUSG00000031596; -.
DR eggNOG; KOG1286; Eukaryota.
DR GeneTree; ENSGT00940000160440; -.
DR HOGENOM; CLU_007946_15_7_1; -.
DR InParanoid; P18581; -.
DR OMA; WFAKTHP; -.
DR OrthoDB; 439017at2759; -.
DR TreeFam; TF315212; -.
DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR BioGRID-ORCS; 11988; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Slc7a2; mouse.
DR PRO; PR:P18581; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P18581; protein.
DR Bgee; ENSMUSG00000031596; Expressed in epithelium of lens and 208 other tissues.
DR ExpressionAtlas; P18581; baseline and differential.
DR Genevisible; P18581; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; ISO:MGI.
DR GO; GO:0061459; F:L-arginine transmembrane transporter activity; IMP:MGI.
DR GO; GO:0015189; F:L-lysine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0000064; F:L-ornithine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0089718; P:amino acid import across plasma membrane; ISO:MGI.
DR GO; GO:0006865; P:amino acid transport; IBA:GO_Central.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:1902475; P:L-alpha-amino acid transmembrane transport; ISO:MGI.
DR GO; GO:0015807; P:L-amino acid transport; ISO:MGI.
DR GO; GO:0097638; P:L-arginine import across plasma membrane; ISO:MGI.
DR GO; GO:1903826; P:L-arginine transmembrane transport; IMP:MGI.
DR GO; GO:1903352; P:L-ornithine transmembrane transport; IBA:GO_Central.
DR GO; GO:0042116; P:macrophage activation; IMP:MGI.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IMP:MGI.
DR GO; GO:0002537; P:nitric oxide production involved in inflammatory response; IMP:MGI.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
DR GO; GO:0043030; P:regulation of macrophage activation; IMP:UniProtKB.
DR InterPro; IPR002293; AA/rel_permease1.
DR InterPro; IPR004755; Cat_AA_permease.
DR InterPro; IPR029485; CAT_C.
DR Pfam; PF13520; AA_permease_2; 1.
DR Pfam; PF13906; AA_permease_C; 1.
DR TIGRFAMs; TIGR00906; 2A0303; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amino-acid transport; Cell membrane; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..657
FT /note="Cationic amino acid transporter 2"
FT /id="PRO_0000054265"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..63
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..163
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..248
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..339
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..409
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..523
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..556
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 557..577
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 578..581
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 603..657
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52569"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52569"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT CARBOHYD 157
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 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 357..397
FT /note="MFPLPRILFAMARDGLLFRFLARVSKRQSPVAATMTAGVIS -> IFPMPRV
FT IYAMAEDGLLFKCLAQINSKTKTPVIATLSSGAVA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:16239143,
FT ECO:0000303|PubMed:1694015"
FT /id="VSP_000025"
FT CONFLICT 142
FT /note="L -> P (in Ref. 5; BAE32720)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="S -> R (in Ref. 5; BAE32720)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="E -> K (in Ref. 5; BAE42415)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="S -> G (in Ref. 1; AAA75250, 2; AAA37372/AAA37350,
FT 3; AAA20397, 4; AAY87029, 5; BAE42415 and 7; AAI27083)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="S -> A (in Ref. 1; AAA75250, 2; AAA37372/AAA37350,
FT 3; AAA20397, 4; AAY87029, 5; BAE42415 and 7; AAI27083)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="M -> I (in Ref. 1; AAA75250 and 5; BAE32720/
FT BAE42415)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="R -> E (in Ref. 1; AAA75250 and 5; BAE32720/
FT BAE42415)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="I -> M (in Ref. 2; AAA37372)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="D -> E (in Ref. 1; AAA75250, 2; AAA37372/AAA37350,
FT 3; AAA20397, 4; AAY87029, 5; BAE42415 and 7; AAI27083)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="V -> A (in Ref. 1; AAA75250, 2; AAA37372/AAA37350,
FT 3; AAA20397, 4; AAY87029, 5; BAE42415 and 7; AAI27083)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="D -> E (in Ref. 1; AAA75250, 2; AAA37372/AAA37350,
FT 3; AAA20397, 4; AAY87029, 5; BAE42415 and 7; AAI27083)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="A -> V (in Ref. 1; AAA75250, 2; AAA37372/AAA37350,
FT 3; AAA20397, 4; AAY87029, 5; BAE42415 and 7; AAI27083)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="A -> V (in Ref. 1; AAA75250, 2; AAA37372/AAA37350,
FT 3; AAA20397, 4; AAY87029, 5; BAE42415 and 7; AAI27083)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 657 AA; 71856 MW; 140CC99D3AB96082 CRC64;
MIPCRAVLTF ARCLIRRKIV TLDSLEDSKL CRCLTTVDLI ALGVGSTLGA GVYVLAGEVA
KADSGPSIVV SFLIAALASV MAGLCYAEFG ARVPKTGSAY LYTYVTVGEL WAFITGWNLI
LSYVIGTSSV ARAWSGTFDE LLNKQIGQFF KTYFKMNYTG LAEYPDFFAV CLVLLLAGLL
SFGVKESAWV NKFFTAINIL VLLFVMVAGF VKGNVANWKI SEEFLKNISA SAREPPSENG
TSIYGAGGFM PYGFTGTLAG AATCFYAFVG FDCIATTGEE VRNPQKAIPI GIVTSLLVCF
MAYFGVSAAL TLMMPYYLLD EKSPLPVAFE YVRWSPAKYV VSAGSLCALS TSLLGSMFPL
PRILFAMARD GLLFRFLARV SKRQSPVAAT MTAGVISAVM AFLFDLKALV DMMSIGTLMA
YSLVAACVLI LRYQPGLCYD QPKYTPEKET LESCTNATLK SESQVTMLQG QGFSLRTLFS
PSALPTRQSA SLVSFLVGFL AFLILGLSIL TTYGVQAIAR LEAWSLALLA LFLVLCVAVI
LTIWRQPQNQ QKVAFMVPFL PFLPAFSILV NIYLMVQLSA DTWIRFSIWM ALGFLIYFAY
GIRHSLEGNP RDEEDDEDAF SDNINAATEE KSAMQANDHH QRNLSLPFIL HEKTSEC
