LMBRL_HUMAN
ID LMBRL_HUMAN Reviewed; 489 AA.
AC Q6UX01; Q969J4; Q96BY8; Q96HN8; Q9NT09; Q9NVE1; Q9NVU9; Q9ULP6;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Protein LMBR1L;
DE AltName: Full=Limb region 1 protein homolog-like;
DE AltName: Full=Lipocalin-1-interacting membrane receptor {ECO:0000303|PubMed:11287427, ECO:0000303|PubMed:23964685};
DE Short=LIMR {ECO:0000303|PubMed:11287427, ECO:0000303|PubMed:23964685};
GN Name=LMBR1L; Synonyms=KIAA1174, LIMR; ORFNames=UNQ458/PRO783;
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 [GENOMIC DNA / MRNA] (ISOFORM 2), FUNCTION, TOPOLOGY,
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP INTERACTION WITH LCN1.
RC TISSUE=Pituitary;
RX PubMed=11287427; DOI=10.1074/jbc.m101762200;
RA Wojnar P., Lechner M., Merschak P., Redl B.;
RT "Molecular cloning of a novel lipocalin-1 interacting human cell membrane
RT receptor using phage display.";
RL J. Biol. Chem. 276:20206-20212(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Teratocarcinoma;
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 MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, Kidney, and Uterus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-489 (ISOFORMS 1/2/4).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP FUNCTION, AND INTERACTION WITH LCN1.
RX PubMed=12591932; DOI=10.1074/jbc.m210922200;
RA Wojnar P., Lechner M., Redl B.;
RT "Antisense down-regulation of lipocalin-interacting membrane receptor
RT expression inhibits cellular internalization of lipocalin-1 in human NT2
RT cells.";
RL J. Biol. Chem. 278:16209-16215(2003).
RN [8]
RP INTERACTION WITH SCGB1A1.
RX PubMed=16423471; DOI=10.1016/j.gene.2005.10.027;
RA Zhang Z., Kim S.J., Chowdhury B., Wang J., Lee Y.C., Tsai P.C., Choi M.,
RA Mukherjee A.B.;
RT "Interaction of uteroglobin with lipocalin-1 receptor suppresses cancer
RT cell motility and invasion.";
RL Gene 369:66-71(2006).
RN [9]
RP INTERACTION WITH LGB, AND SUBCELLULAR LOCATION.
RX PubMed=17991420; DOI=10.1016/j.bbamem.2007.10.010;
RA Fluckinger M., Merschak P., Hermann M., Haertle T., Redl B.;
RT "Lipocalin-interacting-membrane-receptor (LIMR) mediates cellular
RT internalization of beta-lactoglobulin.";
RL Biochim. Biophys. Acta 1778:342-347(2008).
RN [10]
RP FUNCTION, SUBUNIT, INTERACTION WITH LCN1, ABSENCE OF INTERACTION WITH
RP SCGB1A1 AND LGB, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23964685; DOI=10.3109/09687688.2013.823018;
RA Hesselink R.W., Findlay J.B.;
RT "Expression, characterization and ligand specificity of lipocalin-1
RT interacting membrane receptor (LIMR).";
RL Mol. Membr. Biol. 30:327-337(2013).
RN [11]
RP INTERACTION WITH UBAC2; FAF2; VCP; AMFR; ZNRF3; CTNNB1; LRP6; GSK3A AND
RP GSK3B, AND SUBCELLULAR LOCATION.
RX PubMed=31073040; DOI=10.1126/science.aau0812;
RA Choi J.H., Zhong X., McAlpine W., Liao T.C., Zhang D., Fang B., Russell J.,
RA Ludwig S., Nair-Gill E., Zhang Z., Wang K.W., Misawa T., Zhan X., Choi M.,
RA Wang T., Li X., Tang M., Sun Q., Yu L., Murray A.R., Moresco E.M.Y.,
RA Beutler B.;
RT "LMBR1L regulates lymphopoiesis through Wnt/beta-catenin signaling.";
RL Science 364:0-0(2019).
CC -!- FUNCTION: Plays an essential role in lymphocyte development by
CC negatively regulating the canonical Wnt signaling pathway (By
CC similarity). In association with UBAC2 and E3 ubiquitin-protein ligase
CC AMFR, promotes the ubiquitin-mediated degradation of CTNNB1 and Wnt
CC receptors FZD6 and LRP6 (By similarity). LMBR1L stabilizes the beta-
CC catenin destruction complex that is required for regulating CTNNB1
CC levels (By similarity). Acts as a LCN1 receptor and can mediate its
CC endocytosis (PubMed:11287427, PubMed:12591932, PubMed:23964685).
CC {ECO:0000250|UniProtKB:Q9D1E5, ECO:0000269|PubMed:11287427,
CC ECO:0000269|PubMed:12591932, ECO:0000269|PubMed:23964685}.
CC -!- SUBUNIT: Dimer (PubMed:23964685). Can also form higher oligomers
CC (PubMed:23964685). Interacts with LCN1; this interaction mediates the
CC endocytosis of LCN1 (PubMed:11287427, PubMed:12591932,
CC PubMed:23964685). Interacts with UBAC2, FAF2, VCP, AMFR, ZNRF3, CTNNB1,
CC LRP6, GSK3A and GSK3B (PubMed:31073040). Interacts with DVL2 and RNF43
CC (By similarity). Interaction with SCGB1A1 has been observed in
CC PubMed:16423471, but not in PubMed:23964685 (PubMed:16423471,
CC PubMed:23964685). Interaction with LGB which mediates the endocytosis
CC of LGB has been observed in PubMed:17991420, but not in PubMed:23964685
CC (PubMed:17991420, PubMed:23964685). {ECO:0000250|UniProtKB:Q9D1E5,
CC ECO:0000269|PubMed:11287427, ECO:0000269|PubMed:12591932,
CC ECO:0000269|PubMed:16423471, ECO:0000269|PubMed:17991420,
CC ECO:0000269|PubMed:23964685, ECO:0000305|PubMed:31073040}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11287427,
CC ECO:0000269|PubMed:17991420, ECO:0000269|PubMed:31073040}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:11287427}. Endoplasmic reticulum
CC membrane {ECO:0000269|PubMed:31073040}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q6UX01-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6UX01-2; Sequence=VSP_016893;
CC Name=3;
CC IsoId=Q6UX01-3; Sequence=VSP_016894;
CC Name=4;
CC IsoId=Q6UX01-4; Sequence=VSP_016892;
CC Name=5;
CC IsoId=Q6UX01-5; Sequence=VSP_016895, VSP_016896;
CC -!- TISSUE SPECIFICITY: Expressed in testis, pituitary gland, adrenal
CC gland, trachea, placenta, thymus, cerebellum, stomach, mammary gland,
CC spinal cord. A weaker expression is detected in colon, pancreas, and
CC prostate. {ECO:0000269|PubMed:11287427}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal kidney and lung.
CC {ECO:0000269|PubMed:11287427}.
CC -!- SIMILARITY: Belongs to the LIMR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86488.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF260728; AAK60600.1; -; mRNA.
DR EMBL; AF351620; AAK63067.1; -; Genomic_DNA.
DR EMBL; AB033000; BAA86488.1; ALT_INIT; mRNA.
DR EMBL; AY358572; AAQ88935.1; -; mRNA.
DR EMBL; AK001356; BAA91646.1; -; mRNA.
DR EMBL; AK001651; BAA91811.1; -; mRNA.
DR EMBL; BC008337; AAH08337.1; -; mRNA.
DR EMBL; BC015015; AAH15015.1; -; mRNA.
DR EMBL; BC031550; AAH31550.1; -; mRNA.
DR EMBL; AL137599; CAB70835.1; -; mRNA.
DR CCDS; CCDS73466.1; -. [Q6UX01-3]
DR CCDS; CCDS8780.2; -. [Q6UX01-1]
DR PIR; T46306; T46306.
DR RefSeq; NP_001287679.1; NM_001300750.1. [Q6UX01-4]
DR RefSeq; NP_001287680.1; NM_001300751.1. [Q6UX01-3]
DR RefSeq; NP_060583.2; NM_018113.3. [Q6UX01-1]
DR AlphaFoldDB; Q6UX01; -.
DR BioGRID; 120838; 945.
DR IntAct; Q6UX01; 4.
DR MINT; Q6UX01; -.
DR STRING; 9606.ENSP00000267102; -.
DR iPTMnet; Q6UX01; -.
DR PhosphoSitePlus; Q6UX01; -.
DR BioMuta; LMBR1L; -.
DR DMDM; 85681040; -.
DR jPOST; Q6UX01; -.
DR MassIVE; Q6UX01; -.
DR MaxQB; Q6UX01; -.
DR PaxDb; Q6UX01; -.
DR PeptideAtlas; Q6UX01; -.
DR PRIDE; Q6UX01; -.
DR Antibodypedia; 42857; 75 antibodies from 17 providers.
DR DNASU; 55716; -.
DR Ensembl; ENST00000267102.13; ENSP00000267102.8; ENSG00000139636.16. [Q6UX01-1]
DR Ensembl; ENST00000547382.5; ENSP00000447329.1; ENSG00000139636.16. [Q6UX01-3]
DR GeneID; 55716; -.
DR KEGG; hsa:55716; -.
DR MANE-Select; ENST00000267102.13; ENSP00000267102.8; NM_018113.4; NP_060583.2.
DR UCSC; uc001rth.5; human. [Q6UX01-1]
DR CTD; 55716; -.
DR GeneCards; LMBR1L; -.
DR HGNC; HGNC:18268; LMBR1L.
DR HPA; ENSG00000139636; Low tissue specificity.
DR MIM; 610007; gene.
DR neXtProt; NX_Q6UX01; -.
DR OpenTargets; ENSG00000139636; -.
DR PharmGKB; PA142671545; -.
DR VEuPathDB; HostDB:ENSG00000139636; -.
DR eggNOG; KOG3722; Eukaryota.
DR GeneTree; ENSGT00390000007809; -.
DR HOGENOM; CLU_029445_1_0_1; -.
DR InParanoid; Q6UX01; -.
DR OMA; NCSAFEE; -.
DR OrthoDB; 768229at2759; -.
DR PhylomeDB; Q6UX01; -.
DR TreeFam; TF313485; -.
DR PathwayCommons; Q6UX01; -.
DR SignaLink; Q6UX01; -.
DR BioGRID-ORCS; 55716; 11 hits in 1073 CRISPR screens.
DR ChiTaRS; LMBR1L; human.
DR GeneWiki; LMBR1L; -.
DR GenomeRNAi; 55716; -.
DR Pharos; Q6UX01; Tbio.
DR PRO; PR:Q6UX01; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q6UX01; protein.
DR Bgee; ENSG00000139636; Expressed in right testis and 195 other tissues.
DR ExpressionAtlas; Q6UX01; baseline and differential.
DR Genevisible; Q6UX01; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:UniProtKB.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR GO; GO:0070231; P:T cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
DR GO; GO:0042098; P:T cell proliferation; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR008075; LIMR.
DR InterPro; IPR006876; LMBR1-like_membr_prot.
DR PANTHER; PTHR12625; PTHR12625; 1.
DR Pfam; PF04791; LMBR1; 2.
DR PRINTS; PR01692; LIPOCALINIMR.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Endocytosis; Endoplasmic reticulum;
KW Membrane; Receptor; Reference proteome; Transmembrane; Transmembrane helix;
KW Wnt signaling pathway.
FT CHAIN 1..489
FT /note="Protein LMBR1L"
FT /id="PRO_0000053910"
FT TOPO_DOM 1..21
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..114
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..196
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..350
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..431
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..76
FT /note="LCN1-binding"
FT /evidence="ECO:0000269|PubMed:11287427"
FT REGION 1..59
FT /note="Interaction with LGB"
FT /evidence="ECO:0000269|PubMed:17991420"
FT VAR_SEQ 1..52
FT /note="MEAPDYEVLSVREQLFHERIRECIISTLLFATLYILCHIFLTRFKKPAEFTT
FT -> MVNVKALCEPEVSNCWMNVITGTGSVSSPLLVLPQPGPETSLMTGEP (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016892"
FT VAR_SEQ 53..54
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11287427"
FT /id="VSP_016893"
FT VAR_SEQ 336..355
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_016894"
FT VAR_SEQ 363..393
FT /note="LMVSSVVGFYSSPLFRSLRPRWHDTAMTQII -> PSGNPSLPLFSKPVSWD
FT SRPSTSWTLSPLGL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:10574461"
FT /id="VSP_016895"
FT VAR_SEQ 394..489
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:10574461"
FT /id="VSP_016896"
FT CONFLICT 11
FT /note="V -> A (in Ref. 4; BAA91811)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="S -> P (in Ref. 3; AAQ88935)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="M -> T (in Ref. 4; BAA91646)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="V -> L (in Ref. 5; AAH08337)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="G -> V (in Ref. 4; BAA91646)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="F -> L (in Ref. 2; BAA86488)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 55209 MW; 80D169C977F182E2 CRC64;
MEAPDYEVLS VREQLFHERI RECIISTLLF ATLYILCHIF LTRFKKPAEF TTVDDEDATV
NKIALELCTF TLAIALGAVL LLPFSIISNE VLLSLPRNYY IQWLNGSLIH GLWNLVFLFS
NLSLIFLMPF AYFFTESEGF AGSRKGVLGR VYETVVMLML LTLLVLGMVW VASAIVDKNK
ANRESLYDFW EYYLPYLYSC ISFLGVLLLL VCTPLGLARM FSVTGKLLVK PRLLEDLEEQ
LYCSAFEEAA LTRRICNPTS CWLPLDMELL HRQVLALQTQ RVLLEKRRKA SAWQRNLGYP
LAMLCLLVLT GLSVLIVAIH ILELLIDEAA MPRGMQGTSL GQVSFSKLGS FGAVIQVVLI
FYLMVSSVVG FYSSPLFRSL RPRWHDTAMT QIIGNCVCLL VLSSALPVFS RTLGLTRFDL
LGDFGRFNWL GNFYIVFLYN AAFAGLTTLC LVKTFTAAVR AELIRAFGLD RLPLPVSGFP
QASRKTQHQ
