LRAD3_HUMAN
ID LRAD3_HUMAN Reviewed; 345 AA.
AC Q86YD5; B7Z1U3; B9EG81; Q8NBJ0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Low-density lipoprotein receptor class A domain-containing protein 3 {ECO:0000305};
DE Short=LDLR class A domain-containing protein 3;
DE Flags: Precursor;
GN Name=LDLRAD3 {ECO:0000312|HGNC:HGNC:27046}; Synonyms=LRAD3;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=21795536; DOI=10.1523/jneurosci.5065-10.2011;
RA Ranganathan S., Noyes N.C., Migliorini M., Winkles J.A., Battey F.D.,
RA Hyman B.T., Smith E., Yepes M., Mikhailenko I., Strickland D.K.;
RT "LRAD3, a novel low-density lipoprotein receptor family member that
RT modulates amyloid precursor protein trafficking.";
RL J. Neurosci. 31:10836-10846(2011).
RN [7]
RP INTERACTION WITH ITCH; NEDD4 AND NEDD4L, MUTAGENESIS OF PRO-257; TYR-259;
RP PRO-276; PRO-277 AND TYR-278, AND MOTIF.
RX PubMed=26854353; DOI=10.1021/acs.biochem.5b01218;
RA Noyes N.C., Hampton B., Migliorini M., Strickland D.K.;
RT "Regulation of Itch and Nedd4 E3 Ligase Activity and Degradation by
RT LRAD3.";
RL Biochemistry 55:1204-1213(2016).
RN [8]
RP FUNCTION (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION.
RX PubMed=33208938; DOI=10.1038/s41586-020-2915-3;
RA Ma H., Kim A.S., Kafai N.M., Earnest J.T., Shah A.P., Case J.B., Basore K.,
RA Gilliland T.C., Sun C., Nelson C.A., Thackray L.B., Klimstra W.B.,
RA Fremont D.H., Diamond M.S.;
RT "LDLRAD3 is a receptor for Venezuelan equine encephalitis virus.";
RL Nature 588:308-314(2020).
RN [9]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH VENEZUELAN EQUINE
RP ENCEPHALITIS VIRUS SPIKE PROTEINS E1 AND E2 (MICROBIAL INFECTION),
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-33; MET-36; PRO-44 AND ASP-57.
RX PubMed=34646020; DOI=10.1038/s41586-021-03963-9;
RA Basore K., Ma H., Kafai N.M., Mackin S., Kim A.S., Nelson C.A.,
RA Diamond M.S., Fremont D.H.;
RT "Structure of Venezuelan equine encephalitis virus in complex with the
RT LDLRAD3 receptor.";
RL Nature 598:672-676(2021).
RN [10]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH VENEZUELAN EQUINE
RP ENCEPHALITIS VIRUS SPIKE PROTEINS E1 AND E2 (MICROBIAL INFECTION),
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-50.
RX PubMed=34646021; DOI=10.1038/s41586-021-03909-1;
RA Ma B., Huang C., Ma J., Xiang Y., Zhang X.;
RT "Structure of Venezuelan equine encephalitis virus with its receptor
RT LDLRAD3.";
RL Nature 598:677-681(2021).
CC -!- FUNCTION: May influence APP processing, resulting in a decrease in
CC sAPP-alpha production and increased amyloidogenic P3 peptide
CC production. May regulate ITCH and NEDD4 E3 ligase activity and
CC degradation (PubMed:26854353). {ECO:0000250,
CC ECO:0000269|PubMed:26854353}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Venezuelan
CC equine encephalitis virus. {ECO:0000269|PubMed:33208938,
CC ECO:0000269|PubMed:34646020, ECO:0000269|PubMed:34646021}.
CC -!- SUBUNIT: Interacts with APP precursor C-terminus. Interacts directly
CC with ITCH; this interaction promotes ITCH auto-ubiquitination leading
CC to its degradation (PubMed:26854353). Interacts directly with NEDD4;
CC this interaction promotes NEDD4 auto-ubiquitination (PubMed:26854353).
CC Interacts directly with NEDD4L (PubMed:26854353). {ECO:0000250,
CC ECO:0000269|PubMed:26854353}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Venezuelan equine
CC encephalitis virus/VEEV spike proteins E1 and E2.
CC {ECO:0000269|PubMed:34646020, ECO:0000269|PubMed:34646021}.
CC -!- INTERACTION:
CC Q86YD5; P46937: YAP1; NbExp=2; IntAct=EBI-30833221, EBI-1044059;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:33208938,
CC ECO:0000269|PubMed:34646020, ECO:0000269|PubMed:34646021}; Single-pass
CC type I membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86YD5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86YD5-2; Sequence=VSP_056254;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain, lung, skeletal
CC muscle, and pancreas. Expressed at moderate levels in heart, placenta,
CC and kidney but not detected in the liver.
CC {ECO:0000269|PubMed:21795536}.
CC -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
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DR EMBL; AK293930; BAH11629.1; -; mRNA.
DR EMBL; AK075546; BAC11689.1; -; mRNA.
DR EMBL; AC026269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC129502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68127.1; -; Genomic_DNA.
DR EMBL; BC042754; AAH42754.2; -; mRNA.
DR EMBL; BC136286; AAI36287.1; -; mRNA.
DR EMBL; BC143824; AAI43825.1; -; mRNA.
DR CCDS; CCDS31462.1; -. [Q86YD5-1]
DR CCDS; CCDS76394.1; -. [Q86YD5-2]
DR RefSeq; NP_001291192.1; NM_001304263.1. [Q86YD5-2]
DR RefSeq; NP_001291193.1; NM_001304264.1.
DR RefSeq; NP_777562.1; NM_174902.3. [Q86YD5-1]
DR PDB; 7FFF; EM; 3.00 A; D/E/H/M=1-70.
DR PDB; 7FFL; EM; 3.10 A; D/E/H=1-70.
DR PDB; 7FFN; EM; 3.00 A; M=1-70.
DR PDBsum; 7FFF; -.
DR PDBsum; 7FFL; -.
DR PDBsum; 7FFN; -.
DR AlphaFoldDB; Q86YD5; -.
DR SMR; Q86YD5; -.
DR BioGRID; 126803; 10.
DR IntAct; Q86YD5; 2.
DR STRING; 9606.ENSP00000318607; -.
DR GlyGen; Q86YD5; 1 site.
DR iPTMnet; Q86YD5; -.
DR PhosphoSitePlus; Q86YD5; -.
DR BioMuta; LDLRAD3; -.
DR DMDM; 269849675; -.
DR jPOST; Q86YD5; -.
DR MassIVE; Q86YD5; -.
DR PaxDb; Q86YD5; -.
DR PeptideAtlas; Q86YD5; -.
DR PRIDE; Q86YD5; -.
DR ProteomicsDB; 6373; -.
DR ProteomicsDB; 70404; -. [Q86YD5-1]
DR Antibodypedia; 42763; 140 antibodies from 25 providers.
DR DNASU; 143458; -.
DR Ensembl; ENST00000315571.6; ENSP00000318607.5; ENSG00000179241.13. [Q86YD5-1]
DR Ensembl; ENST00000528989.5; ENSP00000433954.1; ENSG00000179241.13. [Q86YD5-2]
DR GeneID; 143458; -.
DR KEGG; hsa:143458; -.
DR MANE-Select; ENST00000315571.6; ENSP00000318607.5; NM_174902.4; NP_777562.1.
DR UCSC; uc001mwk.2; human. [Q86YD5-1]
DR CTD; 143458; -.
DR DisGeNET; 143458; -.
DR GeneCards; LDLRAD3; -.
DR HGNC; HGNC:27046; LDLRAD3.
DR HPA; ENSG00000179241; Low tissue specificity.
DR MIM; 617986; gene.
DR neXtProt; NX_Q86YD5; -.
DR OpenTargets; ENSG00000179241; -.
DR PharmGKB; PA142671556; -.
DR VEuPathDB; HostDB:ENSG00000179241; -.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000160574; -.
DR HOGENOM; CLU_072228_0_0_1; -.
DR InParanoid; Q86YD5; -.
DR OrthoDB; 885061at2759; -.
DR PhylomeDB; Q86YD5; -.
DR TreeFam; TF332096; -.
DR PathwayCommons; Q86YD5; -.
DR BioGRID-ORCS; 143458; 7 hits in 1077 CRISPR screens.
DR ChiTaRS; LDLRAD3; human.
DR GenomeRNAi; 143458; -.
DR Pharos; Q86YD5; Tbio.
DR PRO; PR:Q86YD5; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q86YD5; protein.
DR Bgee; ENSG00000179241; Expressed in parotid gland and 168 other tissues.
DR ExpressionAtlas; Q86YD5; baseline and differential.
DR Genevisible; Q86YD5; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR GO; GO:0070613; P:regulation of protein processing; IEA:Ensembl.
DR CDD; cd00112; LDLa; 3.
DR Gene3D; 4.10.400.10; -; 3.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR Pfam; PF00057; Ldl_recept_a; 3.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00192; LDLa; 3.
DR SUPFAM; SSF57424; SSF57424; 3.
DR PROSITE; PS01209; LDLRA_1; 3.
DR PROSITE; PS50068; LDLRA_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Host-virus interaction; Lipoprotein; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..345
FT /note="Low-density lipoprotein receptor class A domain-
FT containing protein 3"
FT /id="PRO_0000299378"
FT TOPO_DOM 18..173
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..65
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 70..107
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 112..148
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT REGION 270..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 256..259
FT /note="Involved in ITCH interaction"
FT /evidence="ECO:0000269|PubMed:26854353"
FT MOTIF 275..278
FT /note="Involved in ITCH interaction"
FT /evidence="ECO:0000269|PubMed:26854353"
FT COMPBIAS 279..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 37..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 49..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 71..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 78..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 91..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 113..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 120..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 132..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT VAR_SEQ 16..65
FT /note="ESQLLPGNNFTNECNIPGNFMCSNGRCIPGAWQCDGLPDCFDKSDEKECP
FT -> A (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_056254"
FT MUTAGEN 33
FT /note="G->D: Loss of infection by Venezuelan equine
FT encephalitis virus."
FT /evidence="ECO:0000269|PubMed:34646020"
FT MUTAGEN 36
FT /note="M->T: Loss of infection by Venezuelan equine
FT encephalitis virus."
FT /evidence="ECO:0000269|PubMed:34646020"
FT MUTAGEN 44
FT /note="P->R: Loss of infection by Venezuelan equine
FT encephalitis virus."
FT /evidence="ECO:0000269|PubMed:34646020"
FT MUTAGEN 50
FT /note="D->G: Loss of infection by Venezuelan equine
FT encephalitis virus."
FT /evidence="ECO:0000269|PubMed:34646021"
FT MUTAGEN 57
FT /note="D->V: Loss of infection by Venezuelan equine
FT encephalitis virus."
FT /evidence="ECO:0000269|PubMed:34646020"
FT MUTAGEN 257
FT /note="P->A: Does not affect interaction with ITCH; when
FT associated with A-259. Loss of interaction with ITCH; when
FT associated with A-259; A-276; A-277 and A-278."
FT /evidence="ECO:0000269|PubMed:26854353"
FT MUTAGEN 259
FT /note="Y->A: Does not affect interaction with ITCH; when
FT associated with A-257. Loss of interaction with ITCH; when
FT associated with A-257; A-276; A-277 and A-278."
FT /evidence="ECO:0000269|PubMed:26854353"
FT MUTAGEN 276
FT /note="P->A: Does not affect interaction with ITCH; when
FT associated with A-277 and A-278. Loss of interaction with
FT ITCH; when associated with A-257; A-259; A-277 and A-278."
FT /evidence="ECO:0000269|PubMed:26854353"
FT MUTAGEN 277
FT /note="P->A: Does not affect interaction with ITCH; when
FT associated with A-276 and A-278.Loss of interaction with
FT ITCH; when associated with A-257; A-259; A-276 and A-278."
FT /evidence="ECO:0000269|PubMed:26854353"
FT MUTAGEN 278
FT /note="Y->A: Does not affect interaction with ITCH; when
FT associated with A-276 and A-277.Loss of interaction with
FT ITCH; when associated with A-257; A-259; A-276 and A-277."
FT /evidence="ECO:0000269|PubMed:26854353"
FT CONFLICT 204
FT /note="M -> V (in Ref. 5; AAH42754)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="H -> R (in Ref. 5; AAH42754)"
FT /evidence="ECO:0000305"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:7FFN"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:7FFN"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:7FFN"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:7FFN"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:7FFN"
SQ SEQUENCE 345 AA; 37419 MW; 3EB6CADDC5EE9CC4 CRC64;
MWLLGPLCLL LSSAAESQLL PGNNFTNECN IPGNFMCSNG RCIPGAWQCD GLPDCFDKSD
EKECPKAKSK CGPTFFPCAS GIHCIIGRFR CNGFEDCPDG SDEENCTANP LLCSTARYHC
KNGLCIDKSF ICDGQNNCQD NSDEESCESS QEPGSGQVFV TSENQLVYYP SITYAIIGSS
VIFVLVVALL ALVLHHQRKR NNLMTLPVHR LQHPVLLSRL VVLDHPHHCN VTYNVNNGIQ
YVASQAEQNA SEVGSPPSYS EALLDQRPAW YDLPPPPYSS DTESLNQADL PPYRSRSGSA
NSASSQAASS LLSVEDTSHS PGQPGPQEGT AEPRDSEPSQ GTEEV
