DCSTP_MOUSE
ID DCSTP_MOUSE Reviewed; 470 AA.
AC Q7TNJ0; B2RT61; Q6R315; Q7TNI9; Q9D619;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Dendritic cell-specific transmembrane protein;
DE Short=DC-STAMP;
DE Short=mDC-STAMP;
DE AltName: Full=Dendrocyte-expressed seven transmembrane protein;
DE AltName: Full=Transmembrane 7 superfamily member 4;
GN Name=Dcstamp; Synonyms=Tm7sf4;
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] {ECO:0000305, ECO:0000312|EMBL:BAC81438.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RC TISSUE=Macrophage {ECO:0000269|PubMed:15452179};
RX PubMed=15452179; DOI=10.1084/jem.20040518;
RA Kukita T., Wada N., Kukita A., Kakimoto T., Sandra F., Toh K., Nagata K.,
RA Iijima T., Horiuchi M., Matsusaki H., Hieshima K., Yoshie O., Nomiyama H.;
RT "RANKL-induced DC-STAMP is essential for osteoclastogenesis.";
RL J. Exp. Med. 200:941-946(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAR99406.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAR99406.1};
RC TISSUE=Osteoclast {ECO:0000312|EMBL:AAR99406.1};
RA Miyamoto T., Sawatani Y., Suda T.;
RT "Identification and characterization of osteoclast specific molecules.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 SUBCELLULAR LOCATION, GLYCOSYLATION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=15601667; DOI=10.1189/jlb.0804441;
RA Eleveld-Trancikova D., Triantis V., Moulin V., Looman M.W., Wijers M.,
RA Fransen J.A., Lemckert A.A., Havenga M.J., Figdor C.G., Janssen R.A.,
RA Adema G.J.;
RT "The dendritic cell-derived protein DC-STAMP is highly conserved and
RT localizes to the endoplasmic reticulum.";
RL J. Leukoc. Biol. 77:337-343(2005).
RN [6]
RP FUNCTION IN CELL FUSION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2),
RP DISRUPTION PHENOTYPE, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=16061724; DOI=10.1084/jem.20050645;
RA Yagi M., Miyamoto T., Sawatani Y., Iwamoto K., Hosogane N., Fujita N.,
RA Morita K., Ninomiya K., Suzuki T., Miyamoto K., Oike Y., Takeya M.,
RA Toyama Y., Suda T.;
RT "DC-STAMP is essential for cell-cell fusion in osteoclasts and foreign body
RT giant cells.";
RL J. Exp. Med. 202:345-351(2005).
RN [7]
RP FUNCTION IN CELL FUSION, AND DISRUPTION PHENOTYPE.
RX PubMed=16937266; DOI=10.1007/s00774-006-0697-9;
RA Yagi M., Miyamoto T., Toyama Y., Suda T.;
RT "Role of DC-STAMP in cellular fusion of osteoclasts and macrophage giant
RT cells.";
RL J. Bone Miner. Metab. 24:355-358(2006).
RN [8]
RP FUNCTION IN CELL FUSION, AND DISRUPTION PHENOTYPE.
RX PubMed=17164993; DOI=10.3109/s10165-006-0524-0;
RA Miyamoto T.;
RT "The dendritic cell-specific transmembrane protein DC-STAMP is essential
RT for osteoclast fusion and osteoclast bone-resorbing activity.";
RL Mod. Rheumatol. 16:341-342(2006).
RN [9]
RP FUNCTION IN IMMUNE TOLERANCE, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18653699; DOI=10.1093/intimm/dxn082;
RA Sawatani Y., Miyamoto T., Nagai S., Maruya M., Imai J., Miyamoto K.,
RA Fujita N., Ninomiya K., Suzuki T., Iwasaki R., Toyama Y., Shinohara M.,
RA Koyasu S., Suda T.;
RT "The role of DC-STAMP in maintenance of immune tolerance through regulation
RT of dendritic cell function.";
RL Int. Immunol. 20:1259-1268(2008).
RN [10]
RP FUNCTION IN MYELOID DIFFERENTIATION.
RX PubMed=17713547; DOI=10.1038/sj.leu.2404910;
RA Eleveld-Trancikova D., Janssen R.A., Hendriks I.A., Looman M.W., Moulin V.,
RA Jansen B.J., Jansen J.H., Figdor C.G., Adema G.J.;
RT "The DC-derived protein DC-STAMP influences differentiation of myeloid
RT cells.";
RL Leukemia 22:455-459(2008).
RN [11]
RP FUNCTION, INTERACTION WITH OS9, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18952287; DOI=10.1016/j.molimm.2008.06.032;
RA Jansen B.J., Eleveld-Trancikova D., Sanecka A., van Hout-Kuijer M.,
RA Hendriks I.A., Looman M.G., Leusen J.H., Adema G.J.;
RT "OS9 interacts with DC-STAMP and modulates its intracellular localization
RT in response to TLR ligation.";
RL Mol. Immunol. 46:505-515(2009).
RN [12]
RP FUNCTION IN MYELOID DIFFERENTIATION, HOMODIMERIZATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=20039274; DOI=10.1002/jcp.22012;
RA Mensah K.A., Ritchlin C.T., Schwarz E.M.;
RT "RANKL induces heterogeneous DC-STAMP(lo) and DC-STAMP(hi) osteoclast
RT precursors of which the DC-STAMP(lo) precursors are the master fusogens.";
RL J. Cell. Physiol. 223:76-83(2010).
RN [13]
RP FUNCTION IN CELL FUSION, DISRUPTION PHENOTYPE, INDUCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=22337159; DOI=10.1002/jbmr.1575;
RA Miyamoto H., Suzuki T., Miyauchi Y., Iwasaki R., Kobayashi T., Sato Y.,
RA Miyamoto K., Hoshi H., Hashimoto K., Yoshida S., Hao W., Mori T.,
RA Kanagawa H., Katsuyama E., Fujie A., Morioka H., Matsumoto M., Chiba K.,
RA Takeya M., Toyama Y., Miyamoto T.;
RT "Osteoclast stimulatory transmembrane protein and dendritic cell-specific
RT transmembrane protein cooperatively modulate cell-cell fusion to form
RT osteoclasts and foreign body giant cells.";
RL J. Bone Miner. Res. 27:1289-1297(2012).
CC -!- FUNCTION: Probable cell surface receptor that plays several roles in
CC cellular fusion, cell differentiation, bone and immune homeostasis.
CC Plays a role in TNFSF11-mediated osteoclastogenesis. Cooperates with
CC OCSTAMP in modulating cell-cell fusion in both osteoclasts and foreign
CC body giant cells (FBGCs). Participates in osteoclast bone resorption.
CC Involved in inducing the expression of tartrate-resistant acid
CC phosphatase in osteoclast precursors. Plays a role in haematopoietic
CC stem cell differentiation of bone marrow cells toward the myeloid
CC lineage. Inhibits the development of neutrophilic granulocytes. Plays
CC also a role in the regulation of dendritic cell (DC) antigen
CC presentation activity by controlling phagocytic activity. Involved in
CC the maintenance of immune self-tolerance and avoidance of autoimmune
CC reactions. {ECO:0000269|PubMed:15452179, ECO:0000269|PubMed:16061724,
CC ECO:0000269|PubMed:16937266, ECO:0000269|PubMed:17164993,
CC ECO:0000269|PubMed:17713547, ECO:0000269|PubMed:18653699,
CC ECO:0000269|PubMed:18952287, ECO:0000269|PubMed:20039274,
CC ECO:0000269|PubMed:22337159}.
CC -!- SUBUNIT: Interacts with CREB3 (By similarity). Monomer. Homodimer.
CC Isoform 1 interacts (via the C-terminus cytoplasmic tail) with OS9
CC isoform 1 (via the C-terminus tail); the interaction induces DCSTAMP
CC redistribution to the endoplasmic reticulum-Golgi intermediate
CC compartment. Isoform 1 interacts (via the C-terminus cytoplasmic tail)
CC with OS9 isoform 2 (via the C-terminus tail). {ECO:0000250,
CC ECO:0000269|PubMed:18952287}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Endoplasmic reticulum-Golgi intermediate compartment
CC membrane; Multi-pass membrane protein. Endosome. Note=Localized to the
CC cell surface in osteoclasts and undifferentiated monocytes.
CC Intracellular internalized DCSTAMP is detected in a fraction of RANKL-
CC induced osteoclast precursor. Colocalizes with OS9 in the endoplasmic
CC reticulum (ER) of immature dendritic cell (DC). Translocates from the
CC endoplasmic reticulum to the intermediate/Golgi compartment upon
CC maturation of DC in a OS9-dependent manner. Colocalizes with LAMP1 in
CC endosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000269|PubMed:15452179};
CC IsoId=Q7TNJ0-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|Ref.2};
CC IsoId=Q7TNJ0-2; Sequence=VSP_051763;
CC Name=3 {ECO:0000269|PubMed:15452179};
CC IsoId=Q7TNJ0-3; Sequence=VSP_051765;
CC Name=4 {ECO:0000269|Ref.2};
CC IsoId=Q7TNJ0-4; Sequence=VSP_051764;
CC -!- TISSUE SPECIFICITY: Expressed in macrophages and bone marrow dendritic
CC cells (BM-DC). Weakly expressed in the spleen and lymph node. Highly
CC expressed in multi-nuclear osteoclasts compared to mono-nuclear
CC macrophages. Expressed in foreign body giant cells (FBGCs). Isoform 1
CC and isoform 2 are expressed in osteoclasts.
CC {ECO:0000269|PubMed:15601667, ECO:0000269|PubMed:16061724,
CC ECO:0000269|PubMed:22337159}.
CC -!- INDUCTION: Up-regulated by IL4/interleukin-4, macrophage colony-
CC stimulating factor (M-CSF), receptor activator of NF-KB ligand (RANKL),
CC lipopolysaccharide (LPS) and toll-like receptor (TLR). Up-regulated by
CC TNFSF11-induced osteoclast differentiation in combination with TNF-
CC alpha. Down-regulated upon dendritic cell (DC) maturation.
CC {ECO:0000269|PubMed:15452179, ECO:0000269|PubMed:15601667,
CC ECO:0000269|PubMed:16061724, ECO:0000269|PubMed:18952287,
CC ECO:0000269|PubMed:22337159}.
CC -!- DOMAIN: Several domains are necessary for interacting with OS9. The
CC region in the cytoplasmic tail that is necessary for interaction with
CC OS9, is also required for its transport.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:15601667}.
CC -!- DISRUPTION PHENOTYPE: Mice show a lack of osteoclast and foreign body
CC giant cells multi-nuclear formation and a bone-resorbing efficiency
CC reduction. Mice show increased bone mass. Older (>12 months) mice
CC suffered from multisystemic inflammations in the kidney, lung and
CC salivary gland. Mice show autoimmune symptoms, like dendritic cells
CC (DC) with increased phagocytotic activity and antigen presentation.
CC {ECO:0000269|PubMed:16061724, ECO:0000269|PubMed:16937266,
CC ECO:0000269|PubMed:17164993, ECO:0000269|PubMed:18653699,
CC ECO:0000269|PubMed:22337159}.
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DR EMBL; AB109560; BAC81438.1; -; mRNA.
DR EMBL; AB109561; BAC81439.1; -; mRNA.
DR EMBL; AY517483; AAR99406.1; -; mRNA.
DR EMBL; AY517484; AAR99407.1; -; mRNA.
DR EMBL; AY517485; AAR99408.1; -; mRNA.
DR EMBL; AK014697; BAB29508.1; -; mRNA.
DR EMBL; BC139146; AAI39147.1; -; mRNA.
DR CCDS; CCDS27444.1; -. [Q7TNJ0-1]
DR CCDS; CCDS88758.1; -. [Q7TNJ0-3]
DR CCDS; CCDS88759.1; -. [Q7TNJ0-4]
DR RefSeq; NP_001276437.1; NM_001289508.1. [Q7TNJ0-3]
DR RefSeq; NP_001276441.1; NM_001289512.1. [Q7TNJ0-4]
DR RefSeq; NP_083698.1; NM_029422.4. [Q7TNJ0-1]
DR AlphaFoldDB; Q7TNJ0; -.
DR STRING; 10090.ENSMUSP00000022913; -.
DR PhosphoSitePlus; Q7TNJ0; -.
DR PaxDb; Q7TNJ0; -.
DR PRIDE; Q7TNJ0; -.
DR Antibodypedia; 42882; 80 antibodies from 17 providers.
DR DNASU; 75766; -.
DR Ensembl; ENSMUST00000022913; ENSMUSP00000022913; ENSMUSG00000022303. [Q7TNJ0-1]
DR Ensembl; ENSMUST00000227368; ENSMUSP00000154397; ENSMUSG00000022303. [Q7TNJ0-3]
DR Ensembl; ENSMUST00000228556; ENSMUSP00000154362; ENSMUSG00000022303. [Q7TNJ0-4]
DR GeneID; 75766; -.
DR KEGG; mmu:75766; -.
DR UCSC; uc007voi.2; mouse. [Q7TNJ0-1]
DR UCSC; uc007voj.2; mouse. [Q7TNJ0-4]
DR UCSC; uc011zsn.2; mouse. [Q7TNJ0-3]
DR CTD; 81501; -.
DR MGI; MGI:1923016; Dcstamp.
DR VEuPathDB; HostDB:ENSMUSG00000022303; -.
DR eggNOG; ENOG502QWDQ; Eukaryota.
DR GeneTree; ENSGT00940000153269; -.
DR HOGENOM; CLU_046145_0_0_1; -.
DR InParanoid; Q7TNJ0; -.
DR OMA; CFKHLRC; -.
DR OrthoDB; 821078at2759; -.
DR PhylomeDB; Q7TNJ0; -.
DR TreeFam; TF318254; -.
DR BioGRID-ORCS; 75766; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q7TNJ0; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q7TNJ0; protein.
DR Bgee; ENSMUSG00000022303; Expressed in hindlimb long bone and 14 other tissues.
DR ExpressionAtlas; Q7TNJ0; baseline and differential.
DR Genevisible; Q7TNJ0; MM.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071353; P:cellular response to interleukin-4; ISS:UniProtKB.
DR GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; IDA:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
DR GO; GO:0061025; P:membrane fusion; IDA:UniProtKB.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; IDA:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0030316; P:osteoclast differentiation; IMP:UniProtKB.
DR GO; GO:0072675; P:osteoclast fusion; IDA:UniProtKB.
DR GO; GO:0045780; P:positive regulation of bone resorption; IMP:UniProtKB.
DR GO; GO:0034241; P:positive regulation of macrophage fusion; IDA:UniProtKB.
DR GO; GO:0045657; P:positive regulation of monocyte differentiation; IDA:UniProtKB.
DR InterPro; IPR012858; DC_STAMP-like.
DR Pfam; PF07782; DC_STAMP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Differentiation;
KW Endoplasmic reticulum; Endosome; Immunity; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..470
FT /note="Dendritic cell-specific transmembrane protein"
FT /id="PRO_0000072585"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..376
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT VAR_SEQ 95..177
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_051763"
FT VAR_SEQ 344..446
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.2"
FT /id="VSP_051764"
FT VAR_SEQ 344..399
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15452179"
FT /id="VSP_051765"
FT CONFLICT 449
FT /note="F -> L (in Ref. 2; AAR99408 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 53876 MW; 9CCFBB82DFC2BE6E CRC64;
MRLWTLGTSI FLRLWGTYVF PRSPSWLDFI QHLGVCCFVA FLSVSLFSAA FYWILPPVAL
LSSVWMITCV FLCCSKRARC FILLAVLSCG LREGRNALIA AGTGVVIFGH VENIFYNFRG
LLDSMTCNLR AKSFSVHFPL LKRYTEAIQW IYGLATPLNL FDDLVSWNQT LVVSLFSPSH
ALEAHMNDTR GEVLGVLHHM VVTTELLTSV GQKLLALAGL LLILVSTGLF LKRFLGPCGW
KYENVYITKQ FVRFDEKERH QQRPCVLPLN KKERKKYVIV PSLQLTPKEK KTLGLFFLPV
LTYLYMWVLF AAVDYLLYRL ISSMNKQFQS LPGLEVHLKL RGEKQGTQGV VHDSAFNISM
FEPSCIPKPR LSVSETWVPL SIILLTLIIL GLLSSMLMQL KILVSVSFYP KVERERIEYL
HAKLLEKRSK QPLREADGKP SLYFKKIHFW FPVLKMIRKK QTIPANEDDL
