MALR1_HUMAN
ID MALR1_HUMAN Reviewed; 2156 AA.
AC Q5VYJ5; B7ZBP2; R9WAE9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 4.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=MAM and LDL-receptor class A domain-containing protein 1 {ECO:0000312|HGNC:HGNC:24331};
DE Flags: Precursor;
GN Name=MALRD1 {ECO:0000312|HGNC:HGNC:24331};
GN Synonyms=C10orf112 {ECO:0000312|HGNC:HGNC:24331},
GN DIET1 {ECO:0000303|PubMed:23747249};
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 [MRNA], FUNCTION, INTERACTION WITH FGF19, TISSUE
RP SPECIFICITY, AND VARIANTS VAL-666; HIS-793; ASN-887; ASN-1357; ALA-1417 AND
RP ILE-1602.
RX PubMed=23747249; DOI=10.1016/j.cmet.2013.04.007;
RA Vergnes L., Lee J.M., Chin R.G., Auwerx J., Reue K.;
RT "Diet1 functions in the FGF15/19 enterohepatic signaling axis to modulate
RT bile acid and lipid levels.";
RL Cell Metab. 17:916-928(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
CC -!- FUNCTION: Enhances production and/or transport of FGF19 and thus has a
CC role in regulation of bile acid synthesis.
CC {ECO:0000269|PubMed:23747249}.
CC -!- SUBUNIT: Interacts with FGF19. {ECO:0000269|PubMed:23747249}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:A2AJX4}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in the small intestine.
CC {ECO:0000269|PubMed:23747249}.
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DR EMBL; KC843478; AGN95661.1; -; mRNA.
DR EMBL; AL157895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL357520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL450470; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL589943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF455210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS73071.1; -.
DR RefSeq; NP_001135780.2; NM_001142308.2.
DR AlphaFoldDB; Q5VYJ5; -.
DR SMR; Q5VYJ5; -.
DR STRING; 9606.ENSP00000412763; -.
DR GlyGen; Q5VYJ5; 4 sites.
DR iPTMnet; Q5VYJ5; -.
DR PhosphoSitePlus; Q5VYJ5; -.
DR BioMuta; MALRD1; -.
DR DMDM; 259016361; -.
DR EPD; Q5VYJ5; -.
DR jPOST; Q5VYJ5; -.
DR MassIVE; Q5VYJ5; -.
DR PaxDb; Q5VYJ5; -.
DR PeptideAtlas; Q5VYJ5; -.
DR PRIDE; Q5VYJ5; -.
DR ProteomicsDB; 65634; -.
DR Antibodypedia; 62980; 14 antibodies from 6 providers.
DR DNASU; 340895; -.
DR Ensembl; ENST00000454679.7; ENSP00000412763.3; ENSG00000204740.11.
DR GeneID; 340895; -.
DR KEGG; hsa:340895; -.
DR MANE-Select; ENST00000454679.7; ENSP00000412763.3; NM_001142308.3; NP_001135780.2.
DR UCSC; uc031vyw.1; human.
DR CTD; 340895; -.
DR DisGeNET; 340895; -.
DR GeneCards; MALRD1; -.
DR HGNC; HGNC:24331; MALRD1.
DR HPA; ENSG00000204740; Tissue enriched (intestine).
DR MIM; 617715; gene.
DR neXtProt; NX_Q5VYJ5; -.
DR OpenTargets; ENSG00000204740; -.
DR VEuPathDB; HostDB:ENSG00000204740; -.
DR eggNOG; KOG1095; Eukaryota.
DR GeneTree; ENSGT00940000158809; -.
DR HOGENOM; CLU_002270_0_0_1; -.
DR InParanoid; Q5VYJ5; -.
DR OMA; GGDMWTD; -.
DR OrthoDB; 72691at2759; -.
DR TreeFam; TF343455; -.
DR PathwayCommons; Q5VYJ5; -.
DR BioGRID-ORCS; 340895; 1 hit in 182 CRISPR screens.
DR ChiTaRS; MALRD1; human.
DR GenomeRNAi; 340895; -.
DR Pharos; Q5VYJ5; Tbio.
DR PRO; PR:Q5VYJ5; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q5VYJ5; protein.
DR Bgee; ENSG00000204740; Expressed in ileal mucosa and 103 other tissues.
DR ExpressionAtlas; Q5VYJ5; baseline and differential.
DR Genevisible; Q5VYJ5; HS.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0070858; P:negative regulation of bile acid biosynthetic process; IEA:Ensembl.
DR CDD; cd00112; LDLa; 10.
DR CDD; cd06263; MAM; 8.
DR Gene3D; 4.10.400.10; -; 10.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR000998; MAM_dom.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00057; Ldl_recept_a; 6.
DR Pfam; PF00629; MAM; 9.
DR PRINTS; PR00261; LDLRECEPTOR.
DR PRINTS; PR00020; MAMDOMAIN.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00192; LDLa; 10.
DR SMART; SM00137; MAM; 9.
DR SUPFAM; SSF49899; SSF49899; 9.
DR SUPFAM; SSF57424; SSF57424; 10.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01209; LDLRA_1; 7.
DR PROSITE; PS50068; LDLRA_2; 10.
DR PROSITE; PS50060; MAM_2; 9.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Disulfide bond; EGF-like domain; Glycoprotein;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..2156
FT /note="MAM and LDL-receptor class A domain-containing
FT protein 1"
FT /id="PRO_0000328968"
FT TOPO_DOM 32..2076
FT /note="Vesicular"
FT /evidence="ECO:0000305"
FT TRANSMEM 2077..2097
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2098..2156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 33..68
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 71..229
FT /note="MAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 268..427
FT /note="MAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 433..471
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 474..637
FT /note="MAM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 652..816
FT /note="MAM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 822..860
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 863..1024
FT /note="MAM 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 1049..1086
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1088..1256
FT /note="MAM 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 1263..1301
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1305..1465
FT /note="MAM 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 1482..1518
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1519..1676
FT /note="MAM 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 1683..1720
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1727..1892
FT /note="MAM 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 1902..1939
FT /note="LDL-receptor class A 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1946..1982
FT /note="LDL-receptor class A 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1985..2023
FT /note="LDL-receptor class A 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2024..2057
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 813
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1049
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 52..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 434..446
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 441..459
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 453..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 823..837
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 831..850
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 844..859
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1050..1063
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1057..1076
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1070..1085
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1264..1276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1271..1289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1283..1300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1483..1495
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1490..1508
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1502..1517
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1684..1697
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1692..1710
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1704..1719
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1903..1916
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1910..1929
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1923..1938
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1947..1959
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1954..1972
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1966..1981
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1986..1999
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1993..2012
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2006..2022
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2025..2036
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2030..2045
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2047..2056
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VARIANT 666
FT /note="A -> V (in dbSNP:rs16918344)"
FT /evidence="ECO:0000269|PubMed:23747249"
FT /id="VAR_075928"
FT VARIANT 793
FT /note="D -> H (in dbSNP:rs4601653)"
FT /evidence="ECO:0000269|PubMed:23747249"
FT /id="VAR_075929"
FT VARIANT 887
FT /note="S -> N (in dbSNP:rs2358355)"
FT /evidence="ECO:0000269|PubMed:23747249"
FT /id="VAR_075930"
FT VARIANT 1266
FT /note="D -> A (in dbSNP:rs7100382)"
FT /id="VAR_042585"
FT VARIANT 1277
FT /note="I -> V (in dbSNP:rs7100403)"
FT /id="VAR_042586"
FT VARIANT 1357
FT /note="K -> N (in dbSNP:rs1609746)"
FT /evidence="ECO:0000269|PubMed:23747249"
FT /id="VAR_042587"
FT VARIANT 1417
FT /note="V -> A (in dbSNP:rs10827306)"
FT /evidence="ECO:0000269|PubMed:23747249"
FT /id="VAR_042588"
FT VARIANT 1513
FT /note="D -> G (in dbSNP:rs12773592)"
FT /id="VAR_042589"
FT VARIANT 1516
FT /note="E -> K (in dbSNP:rs12771333)"
FT /id="VAR_042590"
FT VARIANT 1602
FT /note="V -> I (in dbSNP:rs10763975)"
FT /evidence="ECO:0000269|PubMed:23747249"
FT /id="VAR_042592"
FT VARIANT 1683
FT /note="L -> I (in dbSNP:rs16918863)"
FT /id="VAR_042594"
FT VARIANT 1721
FT /note="H -> Q (in dbSNP:rs12256835)"
FT /id="VAR_042595"
FT VARIANT 1807
FT /note="M -> T (in dbSNP:rs7100661)"
FT /id="VAR_042596"
FT VARIANT 1895
FT /note="P -> S (in dbSNP:rs16919132)"
FT /id="VAR_042597"
FT VARIANT 1941
FT /note="S -> N (in dbSNP:rs10827628)"
FT /id="VAR_042598"
FT VARIANT 2013
FT /note="M -> R (in dbSNP:rs16919148)"
FT /id="VAR_042599"
SQ SEQUENCE 2156 AA; 241008 MW; 04123CC42AB1460C CRC64;
MLFFLDRMLA FPMNETFCCL WIACVFNSTL AQQGTESFQC DNGVSLPPDS ICDFTDQCGD
SSDERHCLNY ERCDFEDGLC HMTQDQSLQP SWTKRSGMIG LSPPFYDHNG DVSAHFLSLV
SRVDSISSSL RSRVFLPTND QHDCQITFYY FSCQVSGKLM VGLQTACGGP IQHLWQNTAA
LPNQWERNVI KIQSSQRFQV VFEGQMASTY EQDEVIAIDD ISFSSGCLPA NDGILLCQEA
LNAERELCHP DTDLCRFDAT DEELRLCQAC GFEFDMCEWT SEASAGQISW MRTKAREIPA
FESTPQQDQG GDDEGYYVWV GAKHGFTLNH LDSRAYLNSS VCHCLGKSCH LQFYYAMESS
VLRVRLYNNK EEEIFWTYNI STHSQWVKAD VLIPEDLKTF KIIFEGTLLS QRSFIALDHL
WVYACGQTQS RKLCSADEFP CTSGQCIAKE SVCDSRQDCS DESDEDPATC SKHLTCDFES
GFCGWEPFLT EDSHWKLMKG LNNGEHHFPA ADHTANINHG SFIYLEAQRS PGVAKLGSPV
LTKLLTASTP CQVQFWYHLS QHSNLSVFTR TSLDGNLQKQ GKIIRFSESQ WSHAKIDLIA
EAGESTLPFQ LILEATVLSS NATVALDDIS VSQECEISYK SLPRTSTQSK FSKCDFEANS
CDWFEAISGD HFDWIRSSQS ELSADFEHQA PPRDHSLNAS QGHFMFILKK SSSLWQVAKL
QSPTFSQTGP GCILSFWFYN YGLSVGAAEL QLHMENSHDS TVIWRVLYNQ GKQWLEATIQ
LGRLSQPFHL SLDKVSLGIY DGVSAIDDIR FENCTLPLPA ESCEGLDHFW CRHTRACIEK
LRLCDLVDDC GDRTDEVNCA PELQCNFETG ICNWEQDAKD DFDWTRSQGP TPTLNTGPMK
DNTLGTAKGH YLYIESSEPQ AFQDSAALLS PILNATDTKG CTFRFYYHMF GKRIYRLAIY
QRIWSDSRGQ LLWQIFGNQG NRWIRKHLNI SSRQPFQILV EASVGDGFTG DIAIDDLSFM
DCTLYPGNLP ADLPTPPETS VPVTLPPHNC TDNEFICRSD GHCIEKMQKC DFKYDCPDKS
DEASCVMEVC SFEKRSLCKW YQPIPVHLLQ DSNTFRWGLG NGISIHHGEE NHRPSVDHTQ
NTTDGWYLYA DSSNGKFGDT ADILTPIISL TGPKCTLVFW THMNGATVGS LQVLIKKDNV
TSKLWAQTGQ QGAQWKRAEV FLGIRSHTQI VFRAKRGISY IGDVAVDDIS FQDCSPLLSP
ERKCTDHEFM CANKHCIAKD KLCDFVNDCA DNSDETTFIC RTSSGRCDFE FDLCSWKQEK
DEDFDWNLKA SSIPAAGTEP AADHTLGNSS GHYIFIKSLF PQQPMRAARI SSPVISKRSK
NCKIIFHYHM YGNGIGALTL MQVSVTNQTK VLLNLTVEQG NFWRREELSL FGDEDFQLKF
EGRVGKGQRG DIALDDIVLT ENCLSLHDSV QEELAVPLPT GFCPLGYREC HNGKCYRLEQ
SCNFVDNCGD NTDENECGSS CTFEKGWCGW QNSQADNFDW VLGVGSHQSL RPPKDHTLGN
ENGHFMYLEA TAVGLRGDKA HFRSTMWRES SAACTMSFWY FVSAKATGSI QILIKTEKGL
SKVWQESKQN PGNHWQKADI LLGKLRNFEV IFQGIRTRDL GGGAAIDDIE FKNCTTVGEI
SELCPEITDF LCRDKKCIAS HLLCDYKPDC SDRSDEAHCA HYTSTTGSCN FETSSGNWTT
ACSLTQDSED DLDWAIGSRI PAKALIPDSD HTPGSGQHFL YVNSSGSKEG SVARITTSKS
FPASLGMCTV RFWFYMIDPR SMGILKVYTI EESGLNILVW SVIGNKRTGW TYGSVPLSSN
SPFKVAFEAD LDGNEDIFIA LDDISFTPEC VTGGPVPVQP SPCEADQFSC IYTLQCVPLS
GKCDGHEDCI DGSDEMDCPL SPTPPLCSNM EFPCSTDECI PSLLLCDGVP DCHFNEDELI
CSNKSCSNGA LVCASSNSCI PAHQRCDGFA DCMDFQLDES SCSECPLNYC RNGGTCVVEK
NGPMCRCRQG WKGNRCHIKF NPPATDFTYA QNNTWTLLGI GLAFLMTHIT VAVLCFLANR
KVPIRKTEGS GNCAFVNPVY GNWSNPEKTE SSVYSFSNPL YGTTSGSLET LSHHLK
