S36A2_HUMAN
ID S36A2_HUMAN Reviewed; 483 AA.
AC Q495M3; Q495M4; Q495M6; Q6ZWK5; Q7Z6B5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Proton-coupled amino acid transporter 2 {ECO:0000305|PubMed:12809675};
DE Short=Proton/amino acid transporter 2 {ECO:0000303|PubMed:12809675};
DE AltName: Full=Solute carrier family 36 member 2 {ECO:0000312|HGNC:HGNC:18762};
DE AltName: Full=Transmembrane domain rich protein 1 {ECO:0000303|PubMed:15058382};
DE Short=Tramdorin-1 {ECO:0000303|PubMed:15058382};
GN Name=SLC36A2 {ECO:0000312|HGNC:HGNC:18762};
GN Synonyms=PAT2 {ECO:0000303|PubMed:12809675},
GN TRAMD1 {ECO:0000303|PubMed:15058382};
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), FUNCTION, AND TRANSPORTER ACTIVITY.
RC TISSUE=Testis;
RX PubMed=12809675; DOI=10.1016/s0888-7543(03)00099-5;
RA Boll M., Foltz M., Rubio-Aliaga I., Daniel H.;
RT "A cluster of proton/amino acid transporter genes in the human and mouse
RT genomes.";
RL Genomics 82:47-56(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=15058382; DOI=10.1007/s00335-003-2319-3;
RA Bermingham J.R. Jr., Pennington J.;
RT "Organization and expression of the SLC36 cluster of amino acid transporter
RT genes.";
RL Mamm. Genome 15:114-125(2004).
RN [6]
RP VARIANT IG VAL-87, VARIANT HG VAL-87, CHARACTERIZATION OF VARIANT HG
RP VAL-87, FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=19033659; DOI=10.1172/jci36625;
RA Broer S., Bailey C.G., Kowalczuk S., Ng C., Vanslambrouck J.M., Rodgers H.,
RA Auray-Blais C., Cavanaugh J.A., Broer A., Rasko J.E.;
RT "Iminoglycinuria and hyperglycinuria are discrete human phenotypes
RT resulting from complex mutations in proline and glycine transporters.";
RL J. Clin. Invest. 118:3881-3892(2008).
CC -!- FUNCTION: Electrogenic proton/amino acid symporter with a high
CC selectivity for the small side chains amino acids glycine, alanine and
CC proline, where both L- and D-enantiomers are transported. Extension of
CC the backbone length, as in beta-alanine and 4-aminobutanoate or
CC methylation of the amino group, as in sarcosine and N,N-
CC dimethylglycine, are also tolerated but decrease transport efficiency.
CC A free carboxyl group is preferred. {ECO:0000269|PubMed:12809675,
CC ECO:0000269|PubMed:19033659}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine(in) + H(+)(in) = glycine(out) + H(+)(out);
CC Xref=Rhea:RHEA:28899, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305;
CC Evidence={ECO:0000269|PubMed:12809675};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + L-alanine(in) = H(+)(out) + L-alanine(out);
CC Xref=Rhea:RHEA:29443, ChEBI:CHEBI:15378, ChEBI:CHEBI:57972;
CC Evidence={ECO:0000250|UniProtKB:Q8BHK3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-alanine(in) + H(+)(in) = D-alanine(out) + H(+)(out);
CC Xref=Rhea:RHEA:28903, ChEBI:CHEBI:15378, ChEBI:CHEBI:57416;
CC Evidence={ECO:0000250|UniProtKB:Q8BHK3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + L-proline(out) = H(+)(in) + L-proline(in);
CC Xref=Rhea:RHEA:28963, ChEBI:CHEBI:15378, ChEBI:CHEBI:60039;
CC Evidence={ECO:0000269|PubMed:12809675};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-proline(out) + H(+)(out) = D-proline(in) + H(+)(in);
CC Xref=Rhea:RHEA:70643, ChEBI:CHEBI:15378, ChEBI:CHEBI:57726;
CC Evidence={ECO:0000250|UniProtKB:Q8BHK3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxy-L-proline(in) + H(+)(in) = 4-hydroxy-L-proline(out)
CC + H(+)(out); Xref=Rhea:RHEA:70663, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58419; Evidence={ECO:0000250|UniProtKB:Q8BHK3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + L-serine(in) = H(+)(out) + L-serine(out);
CC Xref=Rhea:RHEA:28887, ChEBI:CHEBI:15378, ChEBI:CHEBI:33384;
CC Evidence={ECO:0000250|UniProtKB:Q8BHK3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-serine(out) + H(+)(out) = D-serine(in) + H(+)(in);
CC Xref=Rhea:RHEA:70647, ChEBI:CHEBI:15378, ChEBI:CHEBI:35247;
CC Evidence={ECO:0000250|UniProtKB:Q8BHK3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-alanine(in) + H(+)(in) = beta-alanine(out) + H(+)(out);
CC Xref=Rhea:RHEA:29459, ChEBI:CHEBI:15378, ChEBI:CHEBI:57966;
CC Evidence={ECO:0000250|UniProtKB:Q8BHK3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanoate(in) + H(+)(in) = 4-aminobutanoate(out) +
CC H(+)(out); Xref=Rhea:RHEA:28915, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:59888; Evidence={ECO:0000250|UniProtKB:Q8BHK3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + sarcosine(in) = H(+)(out) + sarcosine(out);
CC Xref=Rhea:RHEA:70655, ChEBI:CHEBI:15378, ChEBI:CHEBI:57433;
CC Evidence={ECO:0000250|UniProtKB:Q8BHK3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + N,N-dimethylglycine(in) = H(+)(out) + N,N-
CC dimethylglycine(out); Xref=Rhea:RHEA:70659, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58251; Evidence={ECO:0000250|UniProtKB:Q8BHK3};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19033659};
CC Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:Q8BHK3}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q8BHK3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q495M3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q495M3-2; Sequence=VSP_032372;
CC Name=3;
CC IsoId=Q495M3-3; Sequence=VSP_032371, VSP_032373;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in kidney and muscle.
CC Expressed in the S1 segment of the proximal tubule close to the
CC glomerulus. {ECO:0000269|PubMed:15058382, ECO:0000269|PubMed:19033659}.
CC -!- DISEASE: Hyperglycinuria (HG) [MIM:138500]: A condition characterized
CC by excess of glycine in the urine. In some cases it is associated with
CC renal colic and renal oxalate stones. {ECO:0000269|PubMed:19033659}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Iminoglycinuria (IG) [MIM:242600]: A disorder of renal tubular
CC reabsorption of glycine and imino acids (proline and hydroxyproline),
CC marked by excessive levels of all three substances in the urine.
CC {ECO:0000269|PubMed:19033659}. Note=The disease is caused by variants
CC affecting distinct genetic loci, including the gene represented in this
CC entry. Mutations in SLC36A2 that retain residual transport activity
CC result in the IG phenotype only when combined with haploinsufficiency
CC of the imino acid transporter SLC6A20 or deficiency of the neutral
CC amino acid transporter SLC6A19. Additional polymorphisms and mutations
CC in SLC6A18 can contribute to iminoglycinuria in some families.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
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DR EMBL; AY162214; AAO11788.1; -; mRNA.
DR EMBL; AK122630; BAC85496.1; -; mRNA.
DR EMBL; CH471062; EAW61678.1; -; Genomic_DNA.
DR EMBL; BC101100; AAI01101.1; -; mRNA.
DR EMBL; BC101101; AAI01102.1; -; mRNA.
DR EMBL; BC101102; AAI01103.1; -; mRNA.
DR EMBL; BC101103; AAI01104.1; -; mRNA.
DR CCDS; CCDS4315.1; -. [Q495M3-1]
DR RefSeq; NP_861441.2; NM_181776.2. [Q495M3-1]
DR RefSeq; XP_016864573.1; XM_017009084.1. [Q495M3-2]
DR AlphaFoldDB; Q495M3; -.
DR IntAct; Q495M3; 2.
DR STRING; 9606.ENSP00000334223; -.
DR DrugBank; DB00260; Cycloserine.
DR GuidetoPHARMACOLOGY; 1162; -.
DR TCDB; 2.A.18.8.6; the amino acid/auxin permease (aaap) family.
DR iPTMnet; Q495M3; -.
DR PhosphoSitePlus; Q495M3; -.
DR BioMuta; SLC36A2; -.
DR DMDM; 121943282; -.
DR jPOST; Q495M3; -.
DR MassIVE; Q495M3; -.
DR PaxDb; Q495M3; -.
DR PeptideAtlas; Q495M3; -.
DR PRIDE; Q495M3; -.
DR ProteomicsDB; 61963; -. [Q495M3-1]
DR ProteomicsDB; 61964; -. [Q495M3-2]
DR ProteomicsDB; 61965; -. [Q495M3-3]
DR Antibodypedia; 28201; 125 antibodies from 24 providers.
DR DNASU; 153201; -.
DR Ensembl; ENST00000335244.9; ENSP00000334223.4; ENSG00000186335.9. [Q495M3-1]
DR GeneID; 153201; -.
DR KEGG; hsa:153201; -.
DR MANE-Select; ENST00000335244.9; ENSP00000334223.4; NM_181776.3; NP_861441.2.
DR UCSC; uc003lty.3; human. [Q495M3-1]
DR CTD; 153201; -.
DR DisGeNET; 153201; -.
DR GeneCards; SLC36A2; -.
DR HGNC; HGNC:18762; SLC36A2.
DR HPA; ENSG00000186335; Group enriched (kidney, skeletal muscle, tongue).
DR MalaCards; SLC36A2; -.
DR MIM; 138500; phenotype.
DR MIM; 242600; phenotype.
DR MIM; 608331; gene.
DR neXtProt; NX_Q495M3; -.
DR OpenTargets; ENSG00000186335; -.
DR Orphanet; 42062; Iminoglycinuria.
DR PharmGKB; PA134899820; -.
DR VEuPathDB; HostDB:ENSG00000186335; -.
DR eggNOG; KOG1304; Eukaryota.
DR GeneTree; ENSGT00940000162044; -.
DR InParanoid; Q495M3; -.
DR OMA; FFIPMER; -.
DR OrthoDB; 464614at2759; -.
DR PhylomeDB; Q495M3; -.
DR TreeFam; TF314873; -.
DR PathwayCommons; Q495M3; -.
DR Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
DR Reactome; R-HSA-428559; Proton-coupled neutral amino acid transporters.
DR Reactome; R-HSA-5619041; Defective SLC36A2 causes iminoglycinuria (IG) and hyperglycinuria (HG).
DR SignaLink; Q495M3; -.
DR SIGNOR; Q495M3; -.
DR BioGRID-ORCS; 153201; 5 hits in 1059 CRISPR screens.
DR ChiTaRS; SLC36A2; human.
DR GeneWiki; SLC36A2; -.
DR GenomeRNAi; 153201; -.
DR Pharos; Q495M3; Tchem.
DR PRO; PR:Q495M3; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q495M3; protein.
DR Bgee; ENSG00000186335; Expressed in quadriceps femoris and 55 other tissues.
DR ExpressionAtlas; Q495M3; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; TAS:Reactome.
DR GO; GO:0005280; F:amino acid:proton symporter activity; IDA:UniProtKB.
DR GO; GO:0015187; F:glycine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015180; F:L-alanine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015193; F:L-proline transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005297; F:proline:proton symporter activity; IDA:UniProtKB.
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:0015816; P:glycine transport; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; TAS:Reactome.
DR GO; GO:0015808; P:L-alanine transport; IBA:GO_Central.
DR GO; GO:0035524; P:proline transmembrane transport; IMP:UniProtKB.
DR GO; GO:0015824; P:proline transport; IEA:Ensembl.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amino-acid transport; Cell membrane; Disease variant;
KW Endoplasmic reticulum; Endosome; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..483
FT /note="Proton-coupled amino acid transporter 2"
FT /id="PRO_0000324819"
FT TOPO_DOM 1..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..81
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..197
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..264
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..349
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..404
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..483
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 26..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..276
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032371"
FT VAR_SEQ 1..198
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032372"
FT VAR_SEQ 277..281
FT /note="ESIGV -> MNDTA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032373"
FT VARIANT 87
FT /note="G -> V (in HG and IG; no effect on localization to
FT the plasma membrane; decreased amino acid:proton symporter
FT activity; no effect on protein reaction kinetics; decreased
FT affinity for proline; 3-fold increase of Km value for
FT proline; decreased affinity for glycine; 5-fold increase of
FT Km for glycine; dbSNP:rs77010315)"
FT /evidence="ECO:0000269|PubMed:19033659"
FT /id="VAR_064795"
FT VARIANT 445
FT /note="A -> V (in dbSNP:rs10042608)"
FT /id="VAR_039887"
FT CONFLICT 156
FT /note="I -> N (in Ref. 1; AAO11788)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="S -> P (in Ref. 1; AAO11788)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="V -> M (in Ref. 2; BAC85496)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="T -> P (in Ref. 2; BAC85496)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 53216 MW; E283B8C6F0C63666 CRC64;
MSVTKSTEGP QGAVAIKLDL MSPPESAKKL ENKDSTFLDE SPSESAGLKK TKGITVFQAL
IHLVKGNMGT GILGLPLAVK NAGILMGPLS LLVMGFIACH CMHILVKCAQ RFCKRLNKPF
MDYGDTVMHG LEANPNAWLQ NHAHWGRHIV SFFLIITQLG FCCVYIVFLA DNLKQVVEAV
NSTTNNCYSN ETVILTPTMD SRLYMLSFLP FLVLLVLIRN LRILTIFSML ANISMLVSLV
IIIQYITQEI PDPSRLPLVA SWKTYPLFFG TAIFSFESIG VVLPLENKMK NARHFPAILS
LGMSIVTSLY IGMAALGYLR FGDDIKASIS LNLPNCWLYQ SVKLLYIAGI LCTYALQFYV
PAEIIIPFAI SRVSTRWALP LDLSIRLVMV CLTCLLAILI PRLDLVISLV GSVSGTALAL
IIPPLLEVTT FYSEGMSPLT IFKDALISIL GFVGFVVGTY QALDELLKSE DSHPFSNSTT
FVR
