FCRL6_HUMAN
ID FCRL6_HUMAN Reviewed; 434 AA.
AC Q6DN72; A1KXW6; A2A4D6; Q6DN73; Q6XRC3; Q6ZNI1;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Fc receptor-like protein 6;
DE Short=FcR-like protein 6;
DE Short=FcRL6;
DE AltName: Full=Fc receptor homolog 6;
DE Short=FcRH6;
DE AltName: Full=IFGP6;
DE Flags: Precursor;
GN Name=FCRL6; Synonyms=FCRH6;
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, INTERACTION WITH PTPN11,
RP TISSUE SPECIFICITY, DOMAIN, PHOSPHORYLATION AT TYR-371, AND MUTAGENESIS OF
RP TYR-356 AND TYR-371.
RX PubMed=17213291; DOI=10.1182/blood-2006-06-030023;
RA Wilson T.J., Presti R.M., Tassi I., Overton E.T., Cella M., Colonna M.;
RT "FcRL6, a new ITIM-bearing receptor on cytolytic cells, is broadly
RT expressed by lymphocytes following HIV-1 infection.";
RL Blood 109:3786-3793(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Tonsil;
RA Ershova S.A.;
RT "Human FcR-like transmembrane receptor IFGP6.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RX PubMed=18991291; DOI=10.1002/eji.200838516;
RA Schreeder D.M., Pan J., Li F.J., Vivier E., Davis R.S.;
RT "FCRL6 distinguishes mature cytotoxic lymphocytes and is upregulated in
RT patients with B-cell chronic lymphocytic leukemia.";
RL Eur. J. Immunol. 38:3159-3166(2008).
RN [6]
RP FUNCTION, AND INTERACTION WITH HLA-DR.
RX PubMed=20519654; DOI=10.4049/jimmunol.1000832;
RA Schreeder D.M., Cannon J.P., Wu J., Li R., Shakhmatov M.A., Davis R.S.;
RT "FcR-like 6 is an MHC class II receptor.";
RL J. Immunol. 185:23-27(2010).
RN [7]
RP INTERACTION WITH PTPN6; PTPN11; INPP5D; INPPL1 AND GRB2, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING, INDUCTION, AND
RP MUTAGENESIS OF TYR-356 AND TYR-371.
RX PubMed=20933011; DOI=10.1016/j.imlet.2010.09.023;
RA Kulemzin S.V., Zamoshnikova A.Y., Yurchenko M.Y., Vitak N.Y.,
RA Najakshin A.M., Fayngerts S.A., Chikaev N.A., Reshetnikova E.S.,
RA Kashirina N.M., Peclo M.M., Rutkevich P.N., Shevelev A.Y.,
RA Yanushevskaya E.V., Baranov K.O., Mamonkin M., Vlasik T.N., Sidorenko S.P.,
RA Taranin A.V., Mechetina L.V.;
RT "FCRL6 receptor: expression and associated proteins.";
RL Immunol. Lett. 134:174-182(2011).
CC -!- FUNCTION: Acts as a MHC class II receptor (PubMed:20519654). When
CC stimulated on its own, does not play a role in cytokine production or
CC the release of cytotoxic granules by NK cells and cytotoxic CD8(+) T
CC cells (PubMed:17213291, PubMed:18991291). Does not act as an Fc
CC receptor (PubMed:18991291). {ECO:0000269|PubMed:17213291,
CC ECO:0000269|PubMed:18991291, ECO:0000269|PubMed:20519654}.
CC -!- SUBUNIT: Interacts (tyrosine phosphorylated) with PTPN11
CC (PubMed:17213291, PubMed:20933011). Interacts (tyrosine phosphorylated)
CC with PTPN6, INPP5D, INPPL1 and GRB2 (PubMed:20933011). Interacts with
CC class II MHC HLA-DR when the alpha chain is associated with a beta-1,
CC beta-4 or a beta-5 but not a beta-3 chain (PubMed:20519654).
CC {ECO:0000269|PubMed:17213291, ECO:0000269|PubMed:20519654,
CC ECO:0000269|PubMed:20933011}.
CC -!- INTERACTION:
CC Q6DN72; Q8N3T1: GALNT15; NbExp=3; IntAct=EBI-23889796, EBI-3925203;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18991291,
CC ECO:0000269|PubMed:20933011}; Single-pass type I membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=FCRL6v1 {ECO:0000303|PubMed:20933011};
CC IsoId=Q6DN72-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6DN72-2; Sequence=VSP_023565, VSP_023568, VSP_023570;
CC Name=3; Synonyms=FCRL6v4 {ECO:0000303|PubMed:20933011};
CC IsoId=Q6DN72-3; Sequence=VSP_023567, VSP_023569;
CC Name=4;
CC IsoId=Q6DN72-4; Sequence=VSP_023566, VSP_023568, VSP_023570;
CC -!- TISSUE SPECIFICITY: Expressed by cytolytic cells including NK cells,
CC effector and effector-memory CD8(+) T-cells, and a subset of NKT cells
CC (at protein level) (PubMed:17213291, PubMed:18991291, PubMed:20933011).
CC Also expressed in gamma delta T cells and in a rare subset of effector
CC CD4(+) T-cells (at protein level) (PubMed:18991291). Expressed in
CC spleen, skin, peripheral blood leukocytes, liver, lung, bone marrow,
CC small intestine and placenta (PubMed:20933011). Expression among T-
CC cells is greatly expanded in HIV-1 infected individuals, and includes
CC not only effector and effector-memory CD8(+) T-cells but also
CC populations of CD4(+) T-cells (PubMed:17213291, PubMed:20933011).
CC Expression among CD8(+) T-cells and NK cells is expanded in individuals
CC with chronic lymphocytic leukemia (CLL) but is reduced in PBMCs from
CC patients with acute (AML), chronic myeloid leukemia (CML) and non-
CC Hodgkin's lymphoma (PubMed:18991291, PubMed:20933011). Expression is
CC higher in PBMCs and/or CD3(+) cells of patients with autoimmune
CC diseases, such as rheumatoid arthritis (RA), systemic lupus
CC erythematosus (SLE) and idiopathic thrombocytopenia purpura (ITP)
CC (PubMed:20933011). In contrast, expression in CD3(+) cells from
CC patients with lupus anticoagulans (LA) is higher (PubMed:20933011).
CC {ECO:0000269|PubMed:17213291, ECO:0000269|PubMed:18991291,
CC ECO:0000269|PubMed:20933011}.
CC -!- INDUCTION: Down-regulated upon stimulation with mitogen
CC phytohaemagglutinin (PHA) or concavalin A in peripheral blood
CC mononuclear cells (PBMCs). {ECO:0000269|PubMed:20933011}.
CC -!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). The
CC phosphorylated ITIM motif is involved in PTPN11 binding.
CC {ECO:0000269|PubMed:17213291}.
CC -!- PTM: Phosphorylated on Tyr residues. Tyrosine phosphorylation induces
CC association with phosphatase PTPN11, PTPN6, INPP5D, INPPL1 and GRB2.
CC {ECO:0000269|PubMed:17213291, ECO:0000269|PubMed:18991291}.
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DR EMBL; AY513661; AAS82876.1; -; mRNA.
DR EMBL; AY212514; AAP47270.1; -; mRNA.
DR EMBL; AY654627; AAT66024.1; -; mRNA.
DR EMBL; AY654628; AAT66025.1; -; mRNA.
DR EMBL; AK131201; BAD18394.1; -; mRNA.
DR EMBL; AL590560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS30912.1; -. [Q6DN72-1]
DR CCDS; CCDS60312.1; -. [Q6DN72-2]
DR RefSeq; NP_001004310.2; NM_001004310.2. [Q6DN72-1]
DR RefSeq; NP_001271146.1; NM_001284217.1. [Q6DN72-2]
DR AlphaFoldDB; Q6DN72; -.
DR SMR; Q6DN72; -.
DR BioGRID; 131251; 2.
DR IntAct; Q6DN72; 1.
DR STRING; 9606.ENSP00000357086; -.
DR GlyGen; Q6DN72; 2 sites.
DR iPTMnet; Q6DN72; -.
DR PhosphoSitePlus; Q6DN72; -.
DR BioMuta; FCRL6; -.
DR DMDM; 134034126; -.
DR MassIVE; Q6DN72; -.
DR PaxDb; Q6DN72; -.
DR PeptideAtlas; Q6DN72; -.
DR PRIDE; Q6DN72; -.
DR ProteomicsDB; 66248; -. [Q6DN72-1]
DR ProteomicsDB; 66249; -. [Q6DN72-2]
DR ProteomicsDB; 66250; -. [Q6DN72-3]
DR TopDownProteomics; Q6DN72-3; -. [Q6DN72-3]
DR Antibodypedia; 47058; 92 antibodies from 15 providers.
DR DNASU; 343413; -.
DR Ensembl; ENST00000321935.10; ENSP00000320625.6; ENSG00000181036.14. [Q6DN72-2]
DR Ensembl; ENST00000339348.9; ENSP00000340949.5; ENSG00000181036.14. [Q6DN72-3]
DR Ensembl; ENST00000368106.4; ENSP00000357086.3; ENSG00000181036.14. [Q6DN72-1]
DR Ensembl; ENST00000392235.7; ENSP00000376068.3; ENSG00000181036.14. [Q6DN72-4]
DR GeneID; 343413; -.
DR KEGG; hsa:343413; -.
DR MANE-Select; ENST00000368106.4; ENSP00000357086.3; NM_001004310.3; NP_001004310.2.
DR UCSC; uc001fuc.4; human. [Q6DN72-1]
DR CTD; 343413; -.
DR DisGeNET; 343413; -.
DR GeneCards; FCRL6; -.
DR HGNC; HGNC:31910; FCRL6.
DR HPA; ENSG00000181036; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 613562; gene.
DR neXtProt; NX_Q6DN72; -.
DR OpenTargets; ENSG00000181036; -.
DR PharmGKB; PA142671770; -.
DR VEuPathDB; HostDB:ENSG00000181036; -.
DR eggNOG; ENOG502RU0I; Eukaryota.
DR GeneTree; ENSGT01050000244808; -.
DR HOGENOM; CLU_023383_5_0_1; -.
DR InParanoid; Q6DN72; -.
DR OMA; FRPWRKA; -.
DR OrthoDB; 866496at2759; -.
DR PhylomeDB; Q6DN72; -.
DR TreeFam; TF335097; -.
DR PathwayCommons; Q6DN72; -.
DR SignaLink; Q6DN72; -.
DR BioGRID-ORCS; 343413; 7 hits in 1054 CRISPR screens.
DR GenomeRNAi; 343413; -.
DR Pharos; Q6DN72; Tbio.
DR PRO; PR:Q6DN72; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6DN72; protein.
DR Bgee; ENSG00000181036; Expressed in granulocyte and 102 other tissues.
DR ExpressionAtlas; Q6DN72; baseline and differential.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042289; F:MHC class II protein binding; IDA:UniProtKB.
DR GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF13895; Ig_2; 3.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..434
FT /note="Fc receptor-like protein 6"
FT /id="PRO_0000280213"
FT TOPO_DOM 20..307
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..434
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..95
FT /note="Ig-like C2-type 1"
FT DOMAIN 111..197
FT /note="Ig-like C2-type 2"
FT DOMAIN 207..293
FT /note="Ig-like C2-type 3"
FT MOTIF 369..374
FT /note="ITIM motif"
FT MOD_RES 371
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:17213291"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 132..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 228..276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1
FT /note="M -> MLPSLGPM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023565"
FT VAR_SEQ 105..199
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_023566"
FT VAR_SEQ 383..397
FT /note="ARSAEFTVGRKDSSI -> GQFYHLCGGEMPAAQ (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_023567"
FT VAR_SEQ 394..406
FT /note="DSSIICAEVRCLQ -> FYHLCGGEMPAAQ (in isoform 2 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_023568"
FT VAR_SEQ 398..434
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_023569"
FT VAR_SEQ 407..434
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_023570"
FT VARIANT 427
FT /note="S -> G (in dbSNP:rs4443889)"
FT /id="VAR_031090"
FT MUTAGEN 356
FT /note="Y->F: No change of phosphorylation implicated in
FT interaction with PTPN11. Loss of interaction with INPPD5,
FT INPPL1 and GRB2."
FT /evidence="ECO:0000269|PubMed:17213291,
FT ECO:0000269|PubMed:20933011"
FT MUTAGEN 371
FT /note="Y->F: Loss of phosphorylation implicated in
FT interaction with PTPN11. Loss of interaction with PTPN11,
FT PTPN6 and INPPL1."
FT /evidence="ECO:0000269|PubMed:17213291,
FT ECO:0000269|PubMed:20933011"
FT CONFLICT 51..52
FT /note="KF -> RL (in Ref. 2; AAP47270)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="L -> P (in Ref. 2; AAP47270)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="L -> P (in Ref. 2; AAP47270)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="R -> Q (in Ref. 2; AAP47270)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="N -> S (in Ref. 2; AAT66025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 434 AA; 47748 MW; 469C1E503AB2CDDE CRC64;
MLLWTAVLLF VPCVGKTVWL YLQAWPNPVF EGDALTLRCQ GWKNTPLSQV KFYRDGKFLH
FSKENQTLSM GAATVQSRGQ YSCSGQVMYI PQTFTQTSET AMVQVQELFP PPVLSAIPSP
EPREGSLVTL RCQTKLHPLR SALRLLFSFH KDGHTLQDRG PHPELCIPGA KEGDSGLYWC
EVAPEGGQVQ KQSPQLEVRV QAPVSRPVLT LHHGPADPAV GDMVQLLCEA QRGSPPILYS
FYLDEKIVGN HSAPCGGTTS LLFPVKSEQD AGNYSCEAEN SVSRERSEPK KLSLKGSQVL
FTPASNWLVP WLPASLLGLM VIAAALLVYV RSWRKAGPLP SQIPPTAPGG EQCPLYANVH
HQKGKDEGVV YSVVHRTSKR SEARSAEFTV GRKDSSIICA EVRCLQPSEV SSTEVNMRSR
TLQEPLSDCE EVLC
