MRP9_HUMAN
ID MRP9_HUMAN Reviewed; 1359 AA.
AC Q96J65; Q49AL2; Q8TAF0; Q8TEY2;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=ATP-binding cassette sub-family C member 12;
DE AltName: Full=Multidrug resistance-associated protein 9;
GN Name=ABCC12; Synonyms=MRP9;
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] (ISOFORMS 2 AND 3), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Liver, Pancreas, and Testis;
RX PubMed=11688999; DOI=10.1006/bbrc.2001.5865;
RA Yabuuchi H., Shimizu H., Takayanagi S., Ishikawa T.;
RT "Multiple splicing variants of two new human ATP-binding cassette
RT transporters, ABCC11 and ABCC12.";
RL Biochem. Biophys. Res. Commun. 288:933-939(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT CYS-1117, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11483364; DOI=10.1016/s0378-1119(01)00572-8;
RA Tammur J., Prades C., Arnould I., Rzhetsky A., Hutchinson A., Adachi M.,
RA Schuetz J.D., Swoboda K.J., Ptacek L.J., Rosier M., Dean M., Allikmets R.;
RT "Two new genes from the human ATP-binding cassette transporter superfamily,
RT ABCC11 and ABCC12, tandemly duplicated on chromosome 16q12.";
RL Gene 273:89-96(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND TISSUE SPECIFICITY.
RX PubMed=12011458; DOI=10.1073/pnas.102187299;
RA Bera T.K., Iavarone C., Kumar V., Lee S., Lee B., Pastan I.;
RT "MRP9, an unusual truncated member of the ABC transporter superfamily, is
RT highly expressed in breast cancer.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6997-7002(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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, SUBCELLULAR LOCATION, AND CAUTION.
RX PubMed=17472575; DOI=10.1042/bj20070292;
RA Ono N., Van der Heijden I., Scheffer G.L., Van de Wetering K.,
RA Van Deemter E., De Haas M., Boerke A., Gadella B.M., De Rooij D.G.,
RA Neefjes J.J., Groothuis T.A., Oomen L., Brocks L., Ishikawa T., Borst P.;
RT "Multidrug resistance-associated protein 9 (ABCC12) is present in mouse and
RT boar sperm.";
RL Biochem. J. 406:31-40(2007).
CC -!- FUNCTION: Probable transporter, its substrate specificity is unknown.
CC {ECO:0000305|PubMed:17472575}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:17472575}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q96J65-1; Sequence=Displayed;
CC Name=2; Synonyms=A, C, D;
CC IsoId=Q96J65-2; Sequence=VSP_021084, VSP_021088, VSP_021092;
CC Name=3; Synonyms=B;
CC IsoId=Q96J65-3; Sequence=VSP_021084, VSP_021088, VSP_021090,
CC VSP_021091;
CC Name=4;
CC IsoId=Q96J65-4; Sequence=VSP_021084, VSP_021086, VSP_021087;
CC Name=5;
CC IsoId=Q96J65-5; Sequence=VSP_021084, VSP_021085, VSP_021089,
CC VSP_021092;
CC -!- TISSUE SPECIFICITY: Expressed in testis (at protein level). Widely
CC expressed at low level (PubMed:11483364, PubMed:11688999,
CC PubMed:12011458, PubMed:17472575). Isoform 5 is specifically expressed
CC in brain, testis and breast cancer cells (PubMed:11483364,
CC PubMed:11688999, PubMed:12011458). {ECO:0000269|PubMed:11483364,
CC ECO:0000269|PubMed:11688999, ECO:0000269|PubMed:12011458,
CC ECO:0000269|PubMed:17472575}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal tissues.
CC {ECO:0000269|PubMed:11688999}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
CC -!- CAUTION: Does not transport any of the organic anions transported by
CC the other multidrug resistance-associated proteins (MRPs) in vesicular
CC transport assays, nor does it confer resistance to cytotoxic agents in
CC intact cell assays. {ECO:0000269|PubMed:17472575}.
CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins;
CC URL="http://abcm2.hegelab.org/search";
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DR EMBL; AF395908; AAL79528.1; -; mRNA.
DR EMBL; AF395909; AAL79529.1; -; mRNA.
DR EMBL; AF411577; AAL99900.1; -; mRNA.
DR EMBL; AF411578; AAL99901.1; -; mRNA.
DR EMBL; AY040220; AAK76740.1; -; mRNA.
DR EMBL; AY196326; AAO40749.1; -; mRNA.
DR EMBL; AC096996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036378; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS10730.1; -. [Q96J65-1]
DR RefSeq; NP_150229.2; NM_033226.2. [Q96J65-1]
DR AlphaFoldDB; Q96J65; -.
DR SMR; Q96J65; -.
DR BioGRID; 125142; 7.
DR IntAct; Q96J65; 3.
DR STRING; 9606.ENSP00000311030; -.
DR TCDB; 3.A.1.208.29; the atp-binding cassette (abc) superfamily.
DR GlyGen; Q96J65; 4 sites.
DR iPTMnet; Q96J65; -.
DR PhosphoSitePlus; Q96J65; -.
DR BioMuta; ABCC12; -.
DR DMDM; 161788999; -.
DR jPOST; Q96J65; -.
DR MassIVE; Q96J65; -.
DR MaxQB; Q96J65; -.
DR PaxDb; Q96J65; -.
DR PeptideAtlas; Q96J65; -.
DR PRIDE; Q96J65; -.
DR ProteomicsDB; 76886; -. [Q96J65-1]
DR ProteomicsDB; 76887; -. [Q96J65-2]
DR ProteomicsDB; 76888; -. [Q96J65-3]
DR ProteomicsDB; 76890; -. [Q96J65-5]
DR Antibodypedia; 28132; 214 antibodies from 28 providers.
DR DNASU; 94160; -.
DR Ensembl; ENST00000497206.6; ENSP00000431232.1; ENSG00000140798.17. [Q96J65-2]
DR Ensembl; ENST00000529084.5; ENSP00000434510.1; ENSG00000140798.17. [Q96J65-4]
DR Ensembl; ENST00000529504.5; ENSP00000433333.1; ENSG00000140798.17. [Q96J65-3]
DR GeneID; 94160; -.
DR KEGG; hsa:94160; -.
DR UCSC; uc002efc.1; human. [Q96J65-1]
DR CTD; 94160; -.
DR DisGeNET; 94160; -.
DR GeneCards; ABCC12; -.
DR HGNC; HGNC:14640; ABCC12.
DR HPA; ENSG00000140798; Tissue enriched (testis).
DR MIM; 607041; gene.
DR neXtProt; NX_Q96J65; -.
DR OpenTargets; ENSG00000140798; -.
DR PharmGKB; PA24394; -.
DR VEuPathDB; HostDB:ENSG00000140798; -.
DR eggNOG; KOG0054; Eukaryota.
DR GeneTree; ENSGT00940000159578; -.
DR HOGENOM; CLU_000604_27_1_1; -.
DR InParanoid; Q96J65; -.
DR OMA; IKGFIFT; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; Q96J65; -.
DR TreeFam; TF105202; -.
DR PathwayCommons; Q96J65; -.
DR SignaLink; Q96J65; -.
DR BioGRID-ORCS; 94160; 11 hits in 1065 CRISPR screens.
DR GeneWiki; ABCC12; -.
DR GenomeRNAi; 94160; -.
DR Pharos; Q96J65; Tbio.
DR PRO; PR:Q96J65; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q96J65; protein.
DR Bgee; ENSG00000140798; Expressed in left testis and 55 other tissues.
DR ExpressionAtlas; Q96J65; baseline and differential.
DR Genevisible; Q96J65; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR030250; ABCC12.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223:SF10; PTHR24223:SF10; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Nucleotide-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1359
FT /note="ATP-binding cassette sub-family C member 12"
FT /id="PRO_0000253578"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 791..811
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 853..873
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 934..954
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1031..1051
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 123..403
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 467..701
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 795..1082
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1120..1354
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 446..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 513..520
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1154..1161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 981
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 142..143
FT /note="VI -> TV (in isoform 2, isoform 3, isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:11688999,
FT ECO:0000303|PubMed:12011458, ECO:0000303|PubMed:15489334"
FT /id="VSP_021084"
FT VAR_SEQ 220..277
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12011458"
FT /id="VSP_021085"
FT VAR_SEQ 572..633
FT /note="YQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQL
FT YLLDDPLSAV -> LGSGASTSLGGRGRGLAWPALSTPTVSSTCWTTPCRPWTPTWGST
FT SLRSALRRRSGERQSSW (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021086"
FT VAR_SEQ 634..1359
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021087"
FT VAR_SEQ 734..736
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11688999"
FT /id="VSP_021088"
FT VAR_SEQ 737..760
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12011458"
FT /id="VSP_021089"
FT VAR_SEQ 892..938
FT /note="ILKSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVV -> H
FT FPQRSPGAQEGGECQPVTLVHPHHLLHAGPGHHSRLWQEGELHHLV (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:11688999"
FT /id="VSP_021090"
FT VAR_SEQ 939..1359
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11688999"
FT /id="VSP_021091"
FT VAR_SEQ 1013..1359
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:11688999,
FT ECO:0000303|PubMed:12011458"
FT /id="VSP_021092"
FT VARIANT 9
FT /note="I -> L (in dbSNP:rs16945901)"
FT /id="VAR_028392"
FT VARIANT 102
FT /note="A -> E (in dbSNP:rs16945874)"
FT /id="VAR_028393"
FT VARIANT 587
FT /note="N -> Y (in dbSNP:rs16945816)"
FT /id="VAR_028394"
FT VARIANT 690
FT /note="E -> V (in dbSNP:rs34135219)"
FT /id="VAR_048139"
FT VARIANT 894
FT /note="K -> M (in dbSNP:rs8057474)"
FT /id="VAR_028395"
FT VARIANT 989
FT /note="T -> S (in dbSNP:rs6500305)"
FT /id="VAR_028396"
FT VARIANT 1013
FT /note="Y -> H (in dbSNP:rs6500304)"
FT /id="VAR_028397"
FT VARIANT 1117
FT /note="R -> C (in dbSNP:rs7193955)"
FT /evidence="ECO:0000269|PubMed:11483364"
FT /id="VAR_028398"
FT VARIANT 1187
FT /note="I -> T (in dbSNP:rs34106426)"
FT /id="VAR_048140"
FT VARIANT 1191
FT /note="E -> A (in dbSNP:rs16945787)"
FT /id="VAR_028399"
FT VARIANT 1349
FT /note="F -> L (in dbSNP:rs12373105)"
FT /id="VAR_028400"
FT CONFLICT 73
FT /note="T -> A (in Ref. 5; BC036378)"
FT /evidence="ECO:0000305"
FT CONFLICT 448..450
FT /note="SRK -> RQE (in Ref. 1; AAL79528/AAL79529/AAL99900/
FT AAL99901)"
FT /evidence="ECO:0000305"
FT CONFLICT 853
FT /note="W -> R (in Ref. 1; AAL79528/AAL79529/AAL99900/
FT AAL99901)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1359 AA; 152297 MW; DA8AF5A3EE9B10E8 CRC64;
MVGEGPYLIS DLDQRGRRRS FAERYDPSLK TMIPVRPCAR LAPNPVDDAG LLSFATFSWL
TPVMVKGYRQ RLTVDTLPPL STYDSSDTNA KRFRVLWDEE VARVGPEKAS LSHVVWKFQR
TRVLMDIVAN ILCIIMAAIG PVILIHQILQ QTERTSGKVW VGIGLCIALF ATEFTKVFFW
ALAWAINYRT AIRLKVALST LVFENLVSFK TLTHISVGEV LNILSSDSYS LFEAALFCPL
PATIPILMVF CAAYAFFILG PTALIGISVY VIFIPVQMFM AKLNSAFRRS AILVTDKRVQ
TMNEFLTCIR LIKMYAWEKS FTNTIQDIRR RERKLLEKAG FVQSGNSALA PIVSTIAIVL
TLSCHILLRR KLTAPVAFSV IAMFNVMKFS IAILPFSIKA MAEANVSLRR MKKILIDKSP
PSYITQPEDP DTVLLLANAT LTWEHEASRK STPKKLQNQK RHLCKKQRSE AYSERSPPAK
GATGPEEQSD SLKSVLHSIS FVVRKGKILG ICGNVGSGKS SLLAALLGQM QLQKGVVAVN
GTLAYVSQQA WIFHGNVREN ILFGEKYDHQ RYQHTVRVCG LQKDLSNLPY GDLTEIGERG
LNLSGGQRQR ISLARAVYSD RQLYLLDDPL SAVDAHVGKH VFEECIKKTL RGKTVVLVTH
QLQFLESCDE VILLEDGEIC EKGTHKELME ERGRYAKLIH NLRGLQFKDP EHLYNAAMVE
AFKESPAERE EDAGIIVLAP GNEKDEGKES ETGSEFVDTK VPEHQLIQTE SPQEGTVTWK
TYHTYIKASG GYLLSLFTVF LFLLMIGSAA FSNWWLGLWL DKGSRMTCGP QGNRTMCEVG
AVLADIGQHV YQWVYTASMV FMLVFGVTKG FVFTKTTLMA SSSLHDTVFD KILKSPMSFF
DTTPTGRLMN RFSKDMDELD VRLPFHAENF LQQFFMVVFI LVILAAVFPA VLLVVASLAV
GFFILLRIFH RGVQELKKVE NVSRSPWFTH ITSSMQGLGI IHAYGKKESC ITYHLLYFNC
ALRWFALRMD VLMNILTFTV ALLVTLSFSS ISTSSKGLSL SYIIQLSGLL QVCVRTGTET
QAKFTSVELL REYISTCVPE CTHPLKVGTC PKDWPSRGEI TFRDYQMRYR DNTPLVLDSL
NLNIQSGQTV GIVGRTGSGK SSLGMALFRL VEPASGTIFI DEVDICILSL EDLRTKLTVI
PQDPVLFVGT VRYNLDPFES HTDEMLWQVL ERTFMRDTIM KLPEKLQAEV TENGENFSVG
ERQLLCVARA LLRNSKIILL DEATASMDSK TDTLVQNTIK DAFKGCTVLT IAHRLNTVLN
CDHVLVMENG KVIEFDKPEV LAEKPDSAFA MLLAAEVRL
