CTR2_HUMAN
ID CTR2_HUMAN Reviewed; 658 AA.
AC P52569; B7ZL54; O15291; O15292; Q14CQ6; Q6NSZ7; Q86TC6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Cationic amino acid transporter 2;
DE Short=CAT-2;
DE Short=CAT2;
DE AltName: Full=Low affinity cationic amino acid transporter 2;
DE AltName: Full=Solute carrier family 7 member 2;
GN Name=SLC7A2; Synonyms=ATRC2, CAT2;
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), AND TISSUE SPECIFICITY.
RC TISSUE=Intestine;
RX PubMed=8954799; DOI=10.1006/geno.1996.0613;
RA Hoshide R., Ikeda Y., Karashima S., Matsuura T., Komaki S., Kishino T.,
RA Niikawa N., Endo F., Matsuda I.;
RT "Molecular cloning, tissue distribution, and chromosomal localization of
RT human cationic amino acid transporter 2 (HCAT2).";
RL Genomics 38:174-178(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 337-469 (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND VARIANT THR-531.
RC TISSUE=Liver;
RX PubMed=9174363; DOI=10.1021/bi962829p;
RA Closs E.I., Graef P., Habermeier A., Cunningham J.M., Foerstermann U.;
RT "Human cationic amino acid transporters hCAT-1, hCAT-2A, and hCAT-2B: three
RT related carriers with distinct transport properties.";
RL Biochemistry 36:6462-6468(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND
RP VARIANT THR-531.
RC TISSUE=Liver;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 313-658 (ISOFORM 2).
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; THR-28; SER-446; SER-464;
RP SER-646 AND SER-647, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Functions as permease involved in the transport of the
CC cationic amino acids (arginine, lysine and ornithine); the affinity for
CC its substrates differs between isoforms created by alternative
CC splicing. Isoform 1 functions as permease that mediates the transport
CC of the cationic amino acids (arginine, lysine and ornithine), and it
CC has much higher affinity for arginine than isoform 2. Isoform 2
CC functions as low-affinity, high capacity permease involved in the
CC transport of the cationic amino acids (arginine, lysine and ornithine)
CC (PubMed:9174363). May play a role in classical or alternative
CC activation of macrophages via its role in arginine transport.
CC {ECO:0000250|UniProtKB:P18581, ECO:0000269|PubMed:9174363}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9174363};
CC Multi-pass membrane protein {ECO:0000269|PubMed:9174363}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=CAT-2B;
CC IsoId=P52569-1; Sequence=Displayed;
CC Name=2; Synonyms=CAT-2A;
CC IsoId=P52569-2; Sequence=VSP_037354, VSP_023354;
CC Name=3;
CC IsoId=P52569-3; Sequence=VSP_037354;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the skeletal muscle,
CC placenta and ovary. Expressed at intermediate levels in the liver and
CC pancreas and at low levels in the kidney and heart.
CC {ECO:0000269|PubMed:8954799}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH69648.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI04906.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI13662.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI43584.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 2]:
CC Sequence=AAB62810.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D29990; BAA06271.1; -; mRNA.
DR EMBL; U76368; AAB62810.1; ALT_FRAME; mRNA.
DR EMBL; U76369; AAB62811.1; -; mRNA.
DR EMBL; AB020863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471080; EAW63813.1; -; Genomic_DNA.
DR EMBL; BC069648; AAH69648.1; ALT_INIT; mRNA.
DR EMBL; BC104905; AAI04906.1; ALT_INIT; mRNA.
DR EMBL; BC113661; AAI13662.1; ALT_INIT; mRNA.
DR EMBL; BC143583; AAI43584.1; ALT_INIT; mRNA.
DR EMBL; AL832016; CAD89909.1; -; mRNA.
DR CCDS; CCDS34852.1; -. [P52569-1]
DR CCDS; CCDS55203.1; -. [P52569-3]
DR CCDS; CCDS6002.2; -. [P52569-2]
DR RefSeq; NP_001008539.3; NM_001008539.3. [P52569-1]
DR RefSeq; NP_001158243.1; NM_001164771.1. [P52569-3]
DR RefSeq; NP_003037.4; NM_003046.5. [P52569-2]
DR RefSeq; XP_005273667.1; XM_005273610.4.
DR RefSeq; XP_005273668.1; XM_005273611.4. [P52569-1]
DR RefSeq; XP_005273669.1; XM_005273612.4. [P52569-1]
DR RefSeq; XP_016869235.1; XM_017013746.1. [P52569-1]
DR RefSeq; XP_016869236.1; XM_017013747.1.
DR AlphaFoldDB; P52569; -.
DR SMR; P52569; -.
DR BioGRID; 112433; 103.
DR IntAct; P52569; 29.
DR MINT; P52569; -.
DR STRING; 9606.ENSP00000004531; -.
DR DrugBank; DB00123; Lysine.
DR DrugBank; DB00129; Ornithine.
DR TCDB; 2.A.3.3.8; the amino acid-polyamine-organocation (apc) family.
DR GlyGen; P52569; 3 sites.
DR iPTMnet; P52569; -.
DR PhosphoSitePlus; P52569; -.
DR SwissPalm; P52569; -.
DR BioMuta; SLC7A2; -.
DR DMDM; 126302539; -.
DR EPD; P52569; -.
DR jPOST; P52569; -.
DR MassIVE; P52569; -.
DR MaxQB; P52569; -.
DR PaxDb; P52569; -.
DR PeptideAtlas; P52569; -.
DR PRIDE; P52569; -.
DR ProteomicsDB; 56491; -. [P52569-1]
DR ProteomicsDB; 56492; -. [P52569-2]
DR ProteomicsDB; 56493; -. [P52569-3]
DR Antibodypedia; 2114; 120 antibodies from 24 providers.
DR DNASU; 6542; -.
DR Ensembl; ENST00000004531.14; ENSP00000004531.10; ENSG00000003989.18. [P52569-3]
DR Ensembl; ENST00000398090.3; ENSP00000381164.3; ENSG00000003989.18. [P52569-2]
DR Ensembl; ENST00000470360.5; ENSP00000419873.1; ENSG00000003989.18. [P52569-2]
DR Ensembl; ENST00000494857.6; ENSP00000419140.2; ENSG00000003989.18. [P52569-1]
DR Ensembl; ENST00000522656.5; ENSP00000430464.1; ENSG00000003989.18. [P52569-1]
DR GeneID; 6542; -.
DR KEGG; hsa:6542; -.
DR MANE-Select; ENST00000494857.6; ENSP00000419140.2; NM_001370338.1; NP_001357267.1.
DR UCSC; uc011kyc.3; human. [P52569-1]
DR CTD; 6542; -.
DR DisGeNET; 6542; -.
DR GeneCards; SLC7A2; -.
DR HGNC; HGNC:11060; SLC7A2.
DR HPA; ENSG00000003989; Tissue enhanced (liver, parathyroid gland).
DR MIM; 601872; gene.
DR neXtProt; NX_P52569; -.
DR OpenTargets; ENSG00000003989; -.
DR PharmGKB; PA35920; -.
DR VEuPathDB; HostDB:ENSG00000003989; -.
DR eggNOG; KOG1286; Eukaryota.
DR GeneTree; ENSGT00940000160440; -.
DR HOGENOM; CLU_007946_15_7_1; -.
DR InParanoid; P52569; -.
DR OMA; WFAKTHP; -.
DR OrthoDB; 439017at2759; -.
DR PhylomeDB; P52569; -.
DR TreeFam; TF315212; -.
DR PathwayCommons; P52569; -.
DR Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
DR SignaLink; P52569; -.
DR BioGRID-ORCS; 6542; 17 hits in 1082 CRISPR screens.
DR ChiTaRS; SLC7A2; human.
DR GeneWiki; SLC7A2; -.
DR GenomeRNAi; 6542; -.
DR Pharos; P52569; Tbio.
DR PRO; PR:P52569; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P52569; protein.
DR Bgee; ENSG00000003989; Expressed in skeletal muscle tissue of rectus abdominis and 158 other tissues.
DR ExpressionAtlas; P52569; baseline and differential.
DR Genevisible; P52569; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0015174; F:basic amino acid transmembrane transporter activity; TAS:ProtInc.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0061459; F:L-arginine transmembrane transporter activity; IDA:ARUK-UCL.
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; IDA:ARUK-UCL.
DR GO; GO:0006865; P:amino acid transport; IBA:GO_Central.
DR GO; GO:1902475; P:L-alpha-amino acid transmembrane transport; IDA:ARUK-UCL.
DR GO; GO:0015807; P:L-amino acid transport; IDA:ARUK-UCL.
DR GO; GO:0097638; P:L-arginine import across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:1903352; P:L-ornithine transmembrane transport; IBA:GO_Central.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
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..658
FT /note="Cationic amino acid transporter 2"
FT /id="PRO_0000054264"
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..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..410
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 432..490
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 512..524
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 525..549
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..557
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 579..582
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 583..603
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 604..658
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 28
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
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 1
FT /note="M -> MKIETSGYNSDKLICRGFIGTPAPPVCDSKFLLSPSSDVRM (in
FT isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005,
FT ECO:0000303|PubMed:9174363"
FT /id="VSP_037354"
FT VAR_SEQ 357..398
FT /note="IFPMPRVIYAMAEDGLLFKCLAQINSKTKTPIIATLSSGAVA -> MFPLPR
FT ILFAMARDGLLFRFLARVSKRQSPVAATLTAGVIS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005,
FT ECO:0000303|PubMed:9174363"
FT /id="VSP_023354"
FT VARIANT 20
FT /note="V -> M (in dbSNP:rs12680645)"
FT /id="VAR_030799"
FT VARIANT 376
FT /note="C -> F (in dbSNP:rs1134975)"
FT /id="VAR_030800"
FT VARIANT 531
FT /note="A -> T (in dbSNP:rs62622371)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9174363"
FT /id="VAR_030801"
FT VARIANT 547
FT /note="Q -> L (in dbSNP:rs1981498)"
FT /id="VAR_058414"
FT CONFLICT 134
FT /note="W -> G (in Ref. 1; BAA06271)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="I -> N (in Ref. 1; BAA06271)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="T -> Y (in Ref. 1; BAA06271)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="Q -> R (in Ref. 1; BAA06271)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="A -> T (in Ref. 1; BAA06271)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="S -> T (in Ref. 1; BAA06271)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="H -> R (in Ref. 6; CAD89909)"
FT /evidence="ECO:0000305"
FT CONFLICT 619
FT /note="D -> V (in Ref. 6; CAD89909)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 658 AA; 71673 MW; 633FD86A333E9208 CRC64;
MIPCRAALTF ARCLIRRKIV TLDSLEDTKL CRCLSTMDLI ALGVGSTLGA GVYVLAGEVA
KADSGPSIVV SFLIAALASV MAGLCYAEFG ARVPKTGSAY LYTYVTVGEL WAFITGWNLI
LSYVIGTSSV ARAWSGTFDE LLSKQIGQFL RTYFRMNYTG LAEYPDFFAV CLILLLAGLL
SFGVKESAWV NKVFTAVNIL VLLFVMVAGF VKGNVANWKI SEEFLKNISA SAREPPSENG
TSIYGAGGFM PYGFTGTLAG AATCFYAFVG FDCIATTGEE VRNPQKAIPI GIVTSLLVCF
MAYFGVSAAL TLMMPYYLLD EKSPLPVAFE YVGWGPAKYV VAAGSLCALS TSLLGSIFPM
PRVIYAMAED GLLFKCLAQI NSKTKTPIIA TLSSGAVAAL MAFLFDLKAL VDMMSIGTLM
AYSLVAACVL ILRYQPGLSY DQPKCSPEKD GLGSSPRVTS KSESQVTMLQ RQGFSMRTLF
CPSLLPTQQS ASLVSFLVGF LAFLVLGLSV LTTYGVHAIT RLEAWSLALL ALFLVLFVAI
VLTIWRQPQN QQKVAFMVPF LPFLPAFSIL VNIYLMVQLS ADTWVRFSIW MAIGFLIYFS
YGIRHSLEGH LRDENNEEDA YPDNVHAAAE EKSAIQANDH HPRNLSSPFI FHEKTSEF
