ID LRP12_HUMAN Reviewed; 859 AA.
AC Q9Y561; A8K137; B4DRQ2;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 196.
DE RecName: Full=Low-density lipoprotein receptor-related protein 12;
DE Short=LDLR-related protein 12;
DE Short=LRP-12;
DE AltName: Full=Suppressor of tumorigenicity 7 protein;
DE Flags: Precursor;
GN Name=LRP12; Synonyms=ST7;
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 {ECO:0000312|EMBL:AAD44360.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=9927190; DOI=10.1038/sj.onc.1202290;
RA Qing J., Wei D., Maher V.M., McCormick J.J.;
RT "Cloning and characterization of a novel gene encoding a putative
RT transmembrane protein with altered expression in some human transformed and
RT tumor-derived cell lines.";
RL Oncogene 18:335-342(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4] {ECO:0000305}
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Retinal pigment epithelium;
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 FUNCTION, SUBCELLULAR LOCATION, AND POSSIBLE INTERACTION WITH RACK1; ZFYVE9
RP AND NMRK2.
RX PubMed=12809483; DOI=10.1021/bi034081y;
RA Battle M.A., Maher V.M., McCormick J.J.;
RT "ST7 is a novel low-density lipoprotein receptor-related protein (LRP) with
RT a cytoplasmic tail that interacts with proteins related to signal
RT transduction pathways.";
RL Biochemistry 42:7270-7282(2003).
RN [7]
RP INVOLVEMENT IN OPDM1.
RX PubMed=31332380; DOI=10.1038/s41588-019-0458-z;
RA Ishiura H., Shibata S., Yoshimura J., Suzuki Y., Qu W., Doi K.,
RA Almansour M.A., Kikuchi J.K., Taira M., Mitsui J., Takahashi Y.,
RA Ichikawa Y., Mano T., Iwata A., Harigaya Y., Matsukawa M.K., Matsukawa T.,
RA Tanaka M., Shirota Y., Ohtomo R., Kowa H., Date H., Mitsue A., Hatsuta H.,
RA Morimoto S., Murayama S., Shiio Y., Saito Y., Mitsutake A., Kawai M.,
RA Sasaki T., Sugiyama Y., Hamada M., Ohtomo G., Terao Y., Nakazato Y.,
RA Takeda A., Sakiyama Y., Umeda-Kameyama Y., Shinmi J., Ogata K., Kohno Y.,
RA Lim S.Y., Tan A.H., Shimizu J., Goto J., Nishino I., Toda T., Morishita S.,
RA Tsuji S.;
RT "Noncoding CGG repeat expansions in neuronal intranuclear inclusion
RT disease, oculopharyngodistal myopathy and an overlapping disease.";
RL Nat. Genet. 51:1222-1232(2019).
CC -!- FUNCTION: Probable receptor, which may be involved in the
CC internalization of lipophilic molecules and/or signal transduction. May
CC act as a tumor suppressor. {ECO:0000269|PubMed:12809483}.
CC -!- SUBUNIT: May interact with RACK1, ZFYVE9 and NMRK2.
CC -!- INTERACTION:
CC Q9Y561; Q9NPI5: NMRK2; NbExp=2; IntAct=EBI-296693, EBI-514059;
CC Q9Y561; P63244: RACK1; NbExp=2; IntAct=EBI-296693, EBI-296739;
CC Q9Y561; O95405: ZFYVE9; NbExp=2; IntAct=EBI-296693, EBI-296817;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12809483}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:12809483}. Membrane,
CC coated pit {ECO:0000269|PubMed:12809483}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y561-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y561-2; Sequence=VSP_040992;
CC -!- TISSUE SPECIFICITY: Widely expressed in heart, skeletal muscle, brain,
CC lung, placenta and pancreas, but not in tissues consisting of a large
CC number of epithelial cells, such as liver and kidney. Expressed at very
CC low levels in a number of tumor-derived cell lines.
CC {ECO:0000269|PubMed:9927190}.
CC -!- DISEASE: Oculopharyngodistal myopathy 1 (OPDM1) [MIM:164310]: A form of
CC oculopharyngodistal myopathy, a muscle disorder characterized by
CC progressive ptosis, external ophthalmoplegia, and weakness of the
CC masseter, facial, pharyngeal, and distal limb muscles. The
CC myopathological features are presence of rimmed vacuoles in the muscle
CC fibers and myopathic changes of differing severity. OPDM1 inheritance
CC pattern is autosomal dominant. {ECO:0000269|PubMed:31332380}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry. The causative mutation is a heterozygous trinucleotide repeat
CC expansion (CGG) in the 5-prime untranslated region of the gene.
CC {ECO:0000269|PubMed:31332380}.
CC -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
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DR EMBL; AF166350; AAD44360.1; -; mRNA.
DR EMBL; AK289752; BAF82441.1; -; mRNA.
DR EMBL; AK299374; BAG61364.1; -; mRNA.
DR EMBL; AC087370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471060; EAW91897.1; -; Genomic_DNA.
DR EMBL; BC032109; AAH32109.1; -; mRNA.
DR CCDS; CCDS47907.1; -. [Q9Y561-2]
DR CCDS; CCDS6303.1; -. [Q9Y561-1]
DR RefSeq; NP_001129175.1; NM_001135703.2. [Q9Y561-2]
DR RefSeq; NP_038465.1; NM_013437.4. [Q9Y561-1]
DR AlphaFoldDB; Q9Y561; -.
DR BioGRID; 119000; 55.
DR IntAct; Q9Y561; 29.
DR MINT; Q9Y561; -.
DR STRING; 9606.ENSP00000276654; -.
DR GlyCosmos; Q9Y561; 6 sites, No reported glycans.
DR GlyGen; Q9Y561; 6 sites.
DR iPTMnet; Q9Y561; -.
DR PhosphoSitePlus; Q9Y561; -.
DR SwissPalm; Q9Y561; -.
DR BioMuta; LRP12; -.
DR DMDM; 25091287; -.
DR EPD; Q9Y561; -.
DR jPOST; Q9Y561; -.
DR MassIVE; Q9Y561; -.
DR MaxQB; Q9Y561; -.
DR PaxDb; 9606-ENSP00000276654; -.
DR PeptideAtlas; Q9Y561; -.
DR ProteomicsDB; 86291; -. [Q9Y561-1]
DR ProteomicsDB; 86292; -. [Q9Y561-2]
DR Antibodypedia; 2508; 211 antibodies from 32 providers.
DR DNASU; 29967; -.
DR Ensembl; ENST00000276654.10; ENSP00000276654.5; ENSG00000147650.12. [Q9Y561-1]
DR Ensembl; ENST00000424843.6; ENSP00000399148.2; ENSG00000147650.12. [Q9Y561-2]
DR GeneID; 29967; -.
DR KEGG; hsa:29967; -.
DR MANE-Select; ENST00000276654.10; ENSP00000276654.5; NM_013437.5; NP_038465.1.
DR UCSC; uc003yma.4; human. [Q9Y561-1]
DR AGR; HGNC:31708; -.
DR CTD; 29967; -.
DR DisGeNET; 29967; -.
DR GeneCards; LRP12; -.
DR HGNC; HGNC:31708; LRP12.
DR HPA; ENSG00000147650; Low tissue specificity.
DR MalaCards; LRP12; -.
DR MIM; 164310; phenotype.
DR MIM; 618299; gene.
DR neXtProt; NX_Q9Y561; -.
DR OpenTargets; ENSG00000147650; -.
DR Orphanet; 98897; Oculopharyngodistal myopathy.
DR PharmGKB; PA134921850; -.
DR VEuPathDB; HostDB:ENSG00000147650; -.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000158307; -.
DR InParanoid; Q9Y561; -.
DR OMA; YTCIPES; -.
DR OrthoDB; 2916406at2759; -.
DR PhylomeDB; Q9Y561; -.
DR TreeFam; TF332149; -.
DR PathwayCommons; Q9Y561; -.
DR Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR SignaLink; Q9Y561; -.
DR BioGRID-ORCS; 29967; 12 hits in 1164 CRISPR screens.
DR ChiTaRS; LRP12; human.
DR GenomeRNAi; 29967; -.
DR Pharos; Q9Y561; Tbio.
DR PRO; PR:Q9Y561; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9Y561; Protein.
DR Bgee; ENSG00000147650; Expressed in stromal cell of endometrium and 174 other cell types or tissues.
DR ExpressionAtlas; Q9Y561; baseline and differential.
DR Genevisible; Q9Y561; HS.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; NAS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; NAS:UniProtKB.
DR GO; GO:0001764; P:neuron migration; IDA:MGI.
DR GO; GO:0031175; P:neuron projection development; IDA:MGI.
DR GO; GO:0040008; P:regulation of growth; NAS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00112; LDLa; 4.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 5.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR PANTHER; PTHR24270:SF47; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 12; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00057; Ldl_recept_a; 4.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00192; LDLa; 5.
DR SUPFAM; SSF57424; LDL receptor-like module; 5.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Coated pit; Disulfide bond; Endocytosis;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..859
FT /note="Low-density lipoprotein receptor-related protein 12"
FT /id="PRO_0000017339"
FT TOPO_DOM 33..492
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..859
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 47..159
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 165..201
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 214..255
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 259..372
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 374..411
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 412..449
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 450..486
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT REGION 623..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..76
FT /evidence="ECO:0000250"
FT DISULFID 103..122
FT /evidence="ECO:0000250"
FT DISULFID 166..178
FT /evidence="ECO:0000250"
FT DISULFID 173..191
FT /evidence="ECO:0000250"
FT DISULFID 185..200
FT /evidence="ECO:0000250"
FT DISULFID 215..232
FT /evidence="ECO:0000250"
FT DISULFID 222..245
FT /evidence="ECO:0000250"
FT DISULFID 239..254
FT /evidence="ECO:0000250"
FT DISULFID 259..285
FT /evidence="ECO:0000250"
FT DISULFID 375..388
FT /evidence="ECO:0000250"
FT DISULFID 382..401
FT /evidence="ECO:0000250"
FT DISULFID 395..410
FT /evidence="ECO:0000250"
FT DISULFID 413..426
FT /evidence="ECO:0000250"
FT DISULFID 420..439
FT /evidence="ECO:0000250"
FT DISULFID 433..448
FT /evidence="ECO:0000250"
FT DISULFID 451..463
FT /evidence="ECO:0000250"
FT DISULFID 458..476
FT /evidence="ECO:0000250"
FT DISULFID 470..485
FT /evidence="ECO:0000250"
FT VAR_SEQ 27..45
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040992"
FT VARIANT 694
FT /note="S -> G (in dbSNP:rs16871494)"
FT /id="VAR_049766"
SQ SEQUENCE 859 AA; 94984 MW; 41A8FD8121E32A92 CRC64;
MACRWSTKES PRWRSALLLL FLAGVYGNGA LAEHSENVHI SGVSTACGET PEQIRAPSGI
ITSPGWPSEY PAKINCSWFI RANPGEIITI SFQDFDIQGS RRCNLDWLTI ETYKNIESYR
ACGSTIPPPY ISSQDHIWIR FHSDDNISRK GFRLAYFSGK SEEPNCACDQ FRCGNGKCIP
EAWKCNNMDE CGDSSDEEIC AKEANPPTAA AFQPCAYNQF QCLSRFTKVY TCLPESLKCD
GNIDCLDLGD EIDCDVPTCG QWLKYFYGTF NSPNYPDFYP PGSNCTWLID TGDHRKVILR
FTDFKLDGTG YGDYVKIYDG LEENPHKLLR VLTAFDSHAP LTVVSSSGQI RVHFCADKVN
AARGFNATYQ VDGFCLPWEI PCGGNWGCYT EQQRCDGYWH CPNGRDETNC TMCQKEEFPC
SRNGVCYPRS DRCNYQNHCP NGSDEKNCFF CQPGNFHCKN NRCVFESWVC DSQDDCGDGS
DEENCPVIVP TRVITAAVIG SLICGLLLVI ALGCTCKLYS LRMFERRSFE TQLSRVEAEL
LRREAPPSYG QLIAQGLIPP VEDFPVCSPN QASVLENLRL AVRSQLGFTS VRLPMAGRSS
NIWNRIFNFA RSRHSGSLAL VSADGDEVVP SQSTSREPER NHTHRSLFSV ESDDTDTENE
RRDMAGASGG VAAPLPQKVP PTTAVEATVG ACASSSTQST RGGHADNGRD VTSVEPPSVS
PARHQLTSAL SRMTQGLRWV RFTLGRSSSL SQNQSPLRQL DNGVSGREDD DDVEMLIPIS
DGSSDFDVND CSRPLLDLAS DQGQGLRQPY NATNPGVRPS NRDGPCERCG IVHTAQIPDT
CLEVTLKNET SDDEALLLC
//
