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   27-MAR-2024, entry version 141.
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   RefSeq; XP_011536865.1; XM_011538563.2.
DR   RefSeq; XP_016875115.1; XM_017019626.1.
DR   AlphaFoldDB; Q6UX01; -.
DR   BioGRID; 120838; 946.
DR   IntAct; Q6UX01; 5.
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; 9606-ENSP00000267102; -.
DR   PeptideAtlas; Q6UX01; -.
DR   Antibodypedia; 42857; 93 antibodies from 18 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   AGR; HGNC:18268; -.
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; QQRRTWW; -.
DR   OrthoDB; 2878909at2759; -.
DR   PhylomeDB; Q6UX01; -.
DR   TreeFam; TF313485; -.
DR   PathwayCommons; Q6UX01; -.
DR   SignaLink; Q6UX01; -.
DR   BioGRID-ORCS; 55716; 13 hits in 1151 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 197 other cell types or tissues.
DR   ExpressionAtlas; Q6UX01; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum 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; LIPOCALIN-1 INTERACTING MEMBRANE RECEPTOR LIMR; 1.
DR   PANTHER; PTHR12625:SF2; PROTEIN LMBR1L; 1.
DR   Pfam; PF04791; LMBR1; 2.
DR   PRINTS; PR01692; LIPOCALINIMR.
DR   Genevisible; Q6UX01; HS.
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
//