B3A3_HUMAN
ID B3A3_HUMAN Reviewed; 1232 AA.
AC P48751; A6H8L2; A8K1Q9; B7ZVX6; B9EGD1; Q6YIQ9;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Anion exchange protein 3;
DE Short=AE 3;
DE Short=Anion exchanger 3;
DE AltName: Full=CAE3/BAE3;
DE AltName: Full=Cardiac/brain band 3-like protein;
DE AltName: Full=Neuronal band 3-like protein;
DE AltName: Full=Solute carrier family 4 member 3;
GN Name=SLC4A3; Synonyms=AE3;
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 BAE3), AND VARIANTS PRO-157 AND
RP ALA-867.
RC TISSUE=Heart;
RX PubMed=7923606; DOI=10.1161/01.res.75.4.603;
RA Yannoukakos D., Stuart-Tilley A., Fernandez H., Fey P., Duyk G.,
RA Alper S.L.;
RT "Molecular cloning, expression, and chromosomal localization of two
RT isoforms of the AE3 anion exchanger from human heart.";
RL Circ. Res. 75:603-614(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CAE3).
RC TISSUE=Heart;
RA Kudo S., Mattei M.-G., Bloor C.M., Fukuda M., Ranney H.M., Xu A.;
RT "Cloning of the characterization of the human cardiac anion exchanger
RT gene.";
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANT PRO-157.
RA Mount D.B.;
RT "Sequence of an alternative splice form of brain AE3.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BAE3), AND VARIANTS PRO-157
RP AND ALA-867.
RC TISSUE=Hippocampus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS PRO-157 AND
RP ALA-867.
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BAE3), AND VARIANTS PRO-157
RP AND ALA-867.
RC TISSUE=Testis;
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).
CC -!- FUNCTION: Plasma membrane anion exchange protein of wide distribution.
CC Mediates at least a part of the Cl(-)/HCO3(-) exchange in cardiac
CC myocytes. Both BAE3 and CAE3 forms transport Cl(-).
CC -!- INTERACTION:
CC P48751; Q12933: TRAF2; NbExp=3; IntAct=EBI-20805570, EBI-355744;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=BAE3;
CC IsoId=P48751-1; Sequence=Displayed;
CC Name=CAE3;
CC IsoId=P48751-2; Sequence=VSP_000462, VSP_000463;
CC Name=3;
CC IsoId=P48751-3; Sequence=VSP_038184;
CC -!- TISSUE SPECIFICITY: Both BAE3 and CAE3 are expressed in failing
CC ventricle.
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000305}.
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DR EMBL; U05596; AAA50748.1; -; mRNA.
DR EMBL; L27213; AAB05850.1; -; mRNA.
DR EMBL; AY142112; AAN34939.1; -; mRNA.
DR EMBL; AK289974; BAF82663.1; -; mRNA.
DR EMBL; AC009955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471063; EAW70778.1; -; Genomic_DNA.
DR EMBL; BC136384; AAI36385.1; -; mRNA.
DR EMBL; BC146656; AAI46657.1; -; mRNA.
DR EMBL; BC171760; AAI71760.1; -; mRNA.
DR CCDS; CCDS2445.1; -. [P48751-1]
DR CCDS; CCDS2446.1; -. [P48751-3]
DR PIR; I38496; I38496.
DR RefSeq; NP_001313488.1; NM_001326559.1. [P48751-3]
DR RefSeq; NP_005061.2; NM_005070.3. [P48751-1]
DR RefSeq; NP_963868.2; NM_201574.2. [P48751-3]
DR RefSeq; XP_005246846.1; XM_005246789.4.
DR AlphaFoldDB; P48751; -.
DR SMR; P48751; -.
DR BioGRID; 112399; 5.
DR IntAct; P48751; 3.
DR MINT; P48751; -.
DR STRING; 9606.ENSP00000273063; -.
DR TCDB; 2.A.31.1.3; the anion exchanger (ae) family.
DR iPTMnet; P48751; -.
DR PhosphoSitePlus; P48751; -.
DR BioMuta; SLC4A3; -.
DR DMDM; 308153414; -.
DR jPOST; P48751; -.
DR MassIVE; P48751; -.
DR MaxQB; P48751; -.
DR PaxDb; P48751; -.
DR PeptideAtlas; P48751; -.
DR PRIDE; P48751; -.
DR ProteomicsDB; 55943; -. [P48751-1]
DR ProteomicsDB; 55944; -. [P48751-2]
DR ProteomicsDB; 55945; -. [P48751-3]
DR Antibodypedia; 52538; 33 antibodies from 14 providers.
DR DNASU; 6508; -.
DR Ensembl; ENST00000273063.10; ENSP00000273063.6; ENSG00000114923.17. [P48751-3]
DR Ensembl; ENST00000317151.7; ENSP00000314006.3; ENSG00000114923.17. [P48751-1]
DR Ensembl; ENST00000358055.8; ENSP00000350756.3; ENSG00000114923.17. [P48751-1]
DR Ensembl; ENST00000373760.6; ENSP00000362865.2; ENSG00000114923.17. [P48751-1]
DR GeneID; 6508; -.
DR KEGG; hsa:6508; -.
DR MANE-Select; ENST00000358055.8; ENSP00000350756.3; NM_005070.4; NP_005061.3.
DR UCSC; uc002vmo.5; human. [P48751-1]
DR CTD; 6508; -.
DR DisGeNET; 6508; -.
DR GeneCards; SLC4A3; -.
DR HGNC; HGNC:11029; SLC4A3.
DR HPA; ENSG00000114923; Group enriched (heart muscle, ovary).
DR MIM; 106195; gene.
DR neXtProt; NX_P48751; -.
DR OpenTargets; ENSG00000114923; -.
DR Orphanet; 51083; Familial short QT syndrome.
DR PharmGKB; PA35897; -.
DR VEuPathDB; HostDB:ENSG00000114923; -.
DR eggNOG; KOG1172; Eukaryota.
DR GeneTree; ENSGT00940000159765; -.
DR HOGENOM; CLU_002289_1_0_1; -.
DR InParanoid; P48751; -.
DR OMA; IMSDQIR; -.
DR OrthoDB; 265068at2759; -.
DR PhylomeDB; P48751; -.
DR TreeFam; TF313630; -.
DR PathwayCommons; P48751; -.
DR Reactome; R-HSA-425381; Bicarbonate transporters.
DR SignaLink; P48751; -.
DR SIGNOR; P48751; -.
DR BioGRID-ORCS; 6508; 10 hits in 1066 CRISPR screens.
DR ChiTaRS; SLC4A3; human.
DR GeneWiki; SLC4A3; -.
DR GenomeRNAi; 6508; -.
DR Pharos; P48751; Tbio.
DR PRO; PR:P48751; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P48751; protein.
DR Bgee; ENSG00000114923; Expressed in apex of heart and 132 other tissues.
DR ExpressionAtlas; P48751; baseline and differential.
DR Genevisible; P48751; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IMP:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015301; F:anion:anion antiporter activity; IBA:GO_Central.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0005452; F:inorganic anion exchanger activity; TAS:Reactome.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015701; P:bicarbonate transport; IMP:ARUK-UCL.
DR GO; GO:0061337; P:cardiac conduction; IMP:ARUK-UCL.
DR GO; GO:0086001; P:cardiac muscle cell action potential; ISS:ARUK-UCL.
DR GO; GO:0050801; P:ion homeostasis; IBA:GO_Central.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR Gene3D; 3.40.930.10; -; 1.
DR InterPro; IPR001717; Anion_exchange.
DR InterPro; IPR002979; Anion_exchange_3.
DR InterPro; IPR018241; Anion_exchange_CS.
DR InterPro; IPR013769; Band3_cytoplasmic_dom.
DR InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR InterPro; IPR003020; HCO3_transpt_euk.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR PANTHER; PTHR11453; PTHR11453; 1.
DR PANTHER; PTHR11453:SF15; PTHR11453:SF15; 1.
DR Pfam; PF07565; Band_3_cyto; 1.
DR Pfam; PF00955; HCO3_cotransp; 1.
DR PRINTS; PR00165; ANIONEXCHNGR.
DR PRINTS; PR01189; ANIONEXHNGR3.
DR PRINTS; PR01231; HCO3TRNSPORT.
DR SUPFAM; SSF55804; SSF55804; 1.
DR TIGRFAMs; TIGR00834; ae; 1.
DR PROSITE; PS00219; ANION_EXCHANGER_1; 1.
DR PROSITE; PS00220; ANION_EXCHANGER_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Anion exchange; Antiport; Ion transport; Lipoprotein;
KW Membrane; Methylation; Palmitate; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1232
FT /note="Anion exchange protein 3"
FT /id="PRO_0000079219"
FT TOPO_DOM 1..708
FT /note="Cytoplasmic"
FT TRANSMEM 709..731
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 737..774
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 794..816
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 826..847
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 893..910
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 911..925
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 926..946
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 980..1002
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1028..1049
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1083..1128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1155..1191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..1232
FT /note="Membrane (anion exchange)"
FT COMPBIAS 9..23
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..113
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..150
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16283"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16283"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23348"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16283"
FT MOD_RES 295
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P16283"
FT LIPID 1165
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..296
FT /note="Missing (in isoform CAE3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_000462"
FT VAR_SEQ 203
FT /note="S -> SRPCSELRDGDGTTDLALSSPRLLCCLP (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_038184"
FT VAR_SEQ 297..299
FT /note="SPS -> MPA (in isoform CAE3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_000463"
FT VARIANT 157
FT /note="H -> P (in dbSNP:rs597306)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7923606,
FT ECO:0000269|Ref.3, ECO:0000269|Ref.6"
FT /id="VAR_059081"
FT VARIANT 226
FT /note="S -> L (in dbSNP:rs36068948)"
FT /id="VAR_055536"
FT VARIANT 867
FT /note="D -> A (in dbSNP:rs635311)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7923606,
FT ECO:0000269|Ref.6"
FT /id="VAR_059082"
FT CONFLICT 118
FT /note="P -> S (in Ref. 7; AAI46657)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="N -> S (in Ref. 7; AAI71760)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="Q -> H (in Ref. 7; AAI46657)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="I -> V (in Ref. 2; AAB05850)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="R -> P (in Ref. 2; AAB05850)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="P -> S (in Ref. 2; AAB05850)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="Q -> K (in Ref. 3; AAN34939)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="S -> G (in Ref. 2; AAB05850)"
FT /evidence="ECO:0000305"
FT CONFLICT 702
FT /note="D -> A (in Ref. 2; AAB05850)"
FT /evidence="ECO:0000305"
FT CONFLICT 812..813
FT /note="GS -> FI (in Ref. 2; AAB05850)"
FT /evidence="ECO:0000305"
FT CONFLICT 822
FT /note="F -> L (in Ref. 2; AAB05850)"
FT /evidence="ECO:0000305"
FT CONFLICT 850
FT /note="H -> R (in Ref. 3; AAN34939)"
FT /evidence="ECO:0000305"
FT CONFLICT 860..863
FT /note="Missing (in Ref. 2; AAB05850)"
FT /evidence="ECO:0000305"
FT CONFLICT 875
FT /note="S -> C (in Ref. 2; AAB05850)"
FT /evidence="ECO:0000305"
FT CONFLICT 885..887
FT /note="SPR -> GPE (in Ref. 2; AAB05850)"
FT /evidence="ECO:0000305"
FT CONFLICT 899
FT /note="L -> P (in Ref. 2; AAB05850)"
FT /evidence="ECO:0000305"
FT CONFLICT 953
FT /note="K -> N (in Ref. 4; BAF82663)"
FT /evidence="ECO:0000305"
FT CONFLICT 983
FT /note="P -> L (in Ref. 7; AAI71760)"
FT /evidence="ECO:0000305"
FT CONFLICT 1052
FT /note="R -> H (in Ref. 4; BAF82663)"
FT /evidence="ECO:0000305"
FT CONFLICT 1054
FT /note="V -> I (in Ref. 3; AAN34939)"
FT /evidence="ECO:0000305"
FT CONFLICT 1096
FT /note="I -> M (in Ref. 2; AAB05850)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1232 AA; 135791 MW; BA0B360E9D30030A CRC64;
MANGVIPPPG GASPLPQVRV PLEEPPLSPD VEEEDDDLGK TLAVSRFGDL ISKPPAWDPE
KPSRSYSERD FEFHRHTSHH THHPLSARLP PPHKLRRLPP TSARHTRRKR KKEKTSAPPS
EGTPPIQEEG GAGVDEEEEE EEEEEGESEA EPVEPPHSGT PQKAKFSIGS DEDDSPGLPG
RAAVTKPLPS VGPHTDKSPQ HSSSSPSPRA RASRLAGEKS RPWSPSASYD LRERLCPGSA
LGNPGGPEQQ VPTDEAEAQM LGSADLDDMK SHRLEDNPGV RRHLVKKPSR TQGGRGSPSG
LAPILRRKKK KKKLDRRPHE VFVELNELML DRSQEPHWRE TARWIKFEED VEEETERWGK
PHVASLSFRS LLELRRTIAH GAALLDLEQT TLPGIAHLVV ETMIVSDQIR PEDRASVLRT
LLLKHSHPND DKDSGFFPRN PSSSSMNSVL GNHHPTPSHG PDGAVPTMAD DLGEPAPLWP
HDPDAKEKPL HMPGGDGHRG KSLKLLEKIP EDAEATVVLV GCVPFLEQPA AAFVRLNEAV
LLESVLEVPV PVRFLFVMLG PSHTSTDYHE LGRSIATLMS DKLFHEAAYQ ADDRQDLLSA
ISEFLDGSIV IPPSEVEGRD LLRSVAAFQR ELLRKRRERE QTKVEMTTRG GYTAPGKELS
LELGGSEATP EDDPLLRTGS VFGGLVRDVR RRYPHYPSDL RDALHSQCVA AVLFIYFAAL
SPAITFGGLL GEKTEGLMGV SELIVSTAVL GVLFSLLGAQ PLLVVGFSGP LLVFEEAFFK
FCRAQDLEYL TGRVWVGLWL VVFVLALVAA EGSFLVRYIS PFTQEIFAFL ISLIFIYETF
YKLYKVFTEH PLLPFYPPEG ALEGSLDAGL EPNGSALPPT EGPPSPRNQP NTALLSLILM
LGTFFIAFFL RKFRNSRFLG GKARRIIGDF GIPISILVMV LVDYSITDTY TQKLTVPTGL
SVTSPDKRSW FIPPLGSARP FPPWMMVAAA VPALLVLILI FMETQITALI VSQKARRLLK
GSGFHLDLLL IGSLGGLCGL FGLPWLTAAT VRSVTHVNAL TVMRTAIAPG DKPQIQEVRE
QRVTGVLIAS LVGLSIVMGA VLRRIPLAVL FGIFLYMGVT SLSGIQLSQR LLLILMPAKH
HPEQPYVTKV KTWRMHLFTC IQLGCIALLW VVKSTAASLA FPFLLLLTVP LRHCLLPRLF
QDRELQALDS EDAEPNFDED GQDEYNELHM PV
