ID   ABCC9_MOUSE             Reviewed;        1546 AA.
AC   P70170; O08902; O08920; P70171;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 2.
DT   24-JAN-2024, entry version 187.
DE   RecName: Full=ATP-binding cassette sub-family C member 9;
DE   AltName: Full=Sulfonylurea receptor 2;
GN   Name=Abcc9; Synonyms=Sur2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SUR2A AND SUR2B).
RC   TISSUE=Heart;
RX   PubMed=8798681; DOI=10.1074/jbc.271.40.24321;
RA   Isomoto S., Kondo C., Yamada M., Matsumoto S., Higashiguchi O., Horio Y.,
RA   Matsuzawa Y., Kurachi Y.;
RT   "A novel sulfonylurea receptor forms with BIR (Kir6.2) a smooth muscle type
RT   ATP-sensitive K+ channel.";
RL   J. Biol. Chem. 271:24321-24324(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SUR2A AND SUR2C).
RX   PubMed=8826984; DOI=10.2337/diab.45.10.1439;
RA   Chutkow W.A., Simon M.C., Le Beau M.M., Burant C.F.;
RT   "Cloning, tissue expression, and chromosomal localization of SUR2, the
RT   putative drug-binding subunit of cardiac, skeletal muscle, and vascular
RT   KATP channels.";
RL   Diabetes 45:1439-1445(1996).
RN   [3]
RP   PROTEIN SEQUENCE OF 493-498, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Subunit of ATP-sensitive potassium channels (KATP). Can form
CC       cardiac and smooth muscle-type KATP channels with KCNJ11. KCNJ11 forms
CC       the channel pore while ABCC9 is required for activation and regulation.
CC   -!- SUBUNIT: Interacts with KCNJ11.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441};
CC       Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=SUR2A;
CC         IsoId=P70170-1; Sequence=Displayed;
CC       Name=SUR2B;
CC         IsoId=P70170-2; Sequence=VSP_000060;
CC       Name=SUR2C;
CC         IsoId=P70170-3; Sequence=VSP_000059;
CC   -!- TISSUE SPECIFICITY: Isoforms SUR2A and SUR2B are found in cerebellum,
CC       eye, atrium, ventricle, urinary bladder and skeletal muscle. Isoform
CC       SUR2B is also found in forebrain, liver, lung, pancreas, kidney,
CC       spleen, stomach, small intestine, colon, uterus, ovary and fat tissue.
CC       Isoform SUR2C is expressed exclusively in the heart.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC       Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR   EMBL; D86037; BAA12969.2; -; mRNA.
DR   EMBL; D86038; BAA12970.2; -; mRNA.
DR   EMBL; AF003531; AAB58753.1; -; mRNA.
DR   EMBL; U97066; AAB58701.1; -; mRNA.
DR   CCDS; CCDS39696.1; -. [P70170-2]
DR   CCDS; CCDS39697.1; -. [P70170-3]
DR   CCDS; CCDS39699.1; -. [P70170-1]
DR   PIR; T42711; T42711.
DR   PIR; T42728; T42728.
DR   RefSeq; NP_001038185.1; NM_001044720.1.
DR   RefSeq; NP_035641.1; NM_011511.2. [P70170-2]
DR   RefSeq; NP_066378.1; NM_021041.2. [P70170-1]
DR   RefSeq; NP_066379.2; NM_021042.2. [P70170-3]
DR   RefSeq; XP_006507011.1; XM_006506948.3.
DR   RefSeq; XP_006507012.1; XM_006506949.3. [P70170-2]
DR   RefSeq; XP_006507013.1; XM_006506950.3. [P70170-2]
DR   RefSeq; XP_006507014.1; XM_006506951.3. [P70170-2]
DR   AlphaFoldDB; P70170; -.
DR   SMR; P70170; -.
DR   BioGRID; 203578; 5.
DR   ComplexPortal; CPX-196; Inward rectifying potassium channel complex, Kir6.2-SUR2A. [P70170-1]
DR   ComplexPortal; CPX-198; Inward rectifying potassium channel complex, Kir6.2-SUR2B. [P70170-2]
DR   CORUM; P70170; -.
DR   STRING; 10090.ENSMUSP00000098390; -.
DR   GlyCosmos; P70170; 2 sites, No reported glycans.
DR   GlyGen; P70170; 2 sites.
DR   iPTMnet; P70170; -.
DR   PhosphoSitePlus; P70170; -.
DR   EPD; P70170; -.
DR   jPOST; P70170; -.
DR   MaxQB; P70170; -.
DR   PaxDb; 10090-ENSMUSP00000084805; -.
DR   ProteomicsDB; 296471; -. [P70170-1]
DR   ProteomicsDB; 297496; -. [P70170-2]
DR   ProteomicsDB; 297497; -. [P70170-3]
DR   ABCD; P70170; 5 sequenced antibodies.
DR   Antibodypedia; 12381; 261 antibodies from 31 providers.
DR   DNASU; 20928; -.
DR   Ensembl; ENSMUST00000073173.12; ENSMUSP00000072914.6; ENSMUSG00000030249.16. [P70170-3]
DR   Ensembl; ENSMUST00000087527.11; ENSMUSP00000084805.5; ENSMUSG00000030249.16. [P70170-1]
DR   Ensembl; ENSMUST00000100827.5; ENSMUSP00000098390.3; ENSMUSG00000030249.16. [P70170-2]
DR   Ensembl; ENSMUST00000205202.3; ENSMUSP00000144779.2; ENSMUSG00000030249.16. [P70170-3]
DR   GeneID; 20928; -.
DR   KEGG; mmu:20928; -.
DR   UCSC; uc009epm.1; mouse. [P70170-1]
DR   UCSC; uc009epo.1; mouse. [P70170-3]
DR   UCSC; uc009epp.1; mouse. [P70170-2]
DR   AGR; MGI:1352630; -.
DR   CTD; 10060; -.
DR   MGI; MGI:1352630; Abcc9.
DR   VEuPathDB; HostDB:ENSMUSG00000030249; -.
DR   eggNOG; KOG0054; Eukaryota.
DR   GeneTree; ENSGT00940000156680; -.
DR   HOGENOM; CLU_000604_27_4_1; -.
DR   InParanoid; P70170; -.
DR   OMA; WLSFWPR; -.
DR   OrthoDB; 3384185at2759; -.
DR   PhylomeDB; P70170; -.
DR   TreeFam; TF105201; -.
DR   Reactome; R-MMU-1296025; ATP sensitive Potassium channels.
DR   Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR   Reactome; R-MMU-5578775; Ion homeostasis.
DR   BioGRID-ORCS; 20928; 1 hit in 77 CRISPR screens.
DR   ChiTaRS; Abcc9; mouse.
DR   PRO; PR:P70170; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; P70170; Protein.
DR   Bgee; ENSMUSG00000030249; Expressed in triceps brachii and 218 other cell types or tissues.
DR   ExpressionAtlas; P70170; baseline and differential.
DR   GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR   GO; GO:0008282; C:inward rectifying potassium channel; ISO:ComplexPortal.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0030017; C:sarcomere; IDA:MGI.
DR   GO; GO:0030315; C:T-tubule; ISO:MGI.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISO:MGI.
DR   GO; GO:1901363; F:heterocyclic compound binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0005267; F:potassium channel activity; IEA:Ensembl.
DR   GO; GO:0015459; F:potassium channel regulator activity; ISO:MGI.
DR   GO; GO:0008281; F:sulfonylurea receptor activity; ISO:MGI.
DR   GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR   GO; GO:0001508; P:action potential; IMP:MGI.
DR   GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR   GO; GO:0061337; P:cardiac conduction; ISO:MGI.
DR   GO; GO:0086003; P:cardiac muscle cell contraction; IMP:MGI.
DR   GO; GO:0072359; P:circulatory system development; IMP:MGI.
DR   GO; GO:0060976; P:coronary vasculature development; IGI:MGI.
DR   GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR   GO; GO:0048144; P:fibroblast proliferation; IGI:MGI.
DR   GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR   GO; GO:0098662; P:inorganic cation transmembrane transport; ISO:MGI.
DR   GO; GO:0098655; P:monoatomic cation transmembrane transport; ISO:MGI.
DR   GO; GO:0045776; P:negative regulation of blood pressure; IMP:MGI.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; ISO:ComplexPortal.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; ISO:MGI.
DR   GO; GO:0006813; P:potassium ion transport; ISO:MGI.
DR   GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR   GO; GO:0033198; P:response to ATP; IMP:MGI.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IGI:MGI.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   CDD; cd18591; ABC_6TM_SUR1_D1_like; 1.
DR   CDD; cd18602; ABC_6TM_SUR1_D2_like; 1.
DR   CDD; cd03290; ABCC_SUR1_N; 1.
DR   CDD; cd03288; ABCC_SUR2; 1.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR000388; ABCC8/9.
DR   InterPro; IPR001475; ABCC9.
DR   InterPro; IPR047080; ABCC9_ATP-bd_dom1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR   PANTHER; PTHR24223:SF173; ATP-BINDING CASSETTE SUB-FAMILY C MEMBER 9; 1.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   PRINTS; PR01094; SULFNYLUR2.
DR   PRINTS; PR01092; SULFNYLUREAR.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR   Genevisible; P70170; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Direct protein sequencing; Glycoprotein;
KW   Membrane; Nucleotide-binding; Receptor; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1546
FT                   /note="ATP-binding cassette sub-family C member 9"
FT                   /id="PRO_0000093403"
FT   TOPO_DOM        1..30
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..51
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        52..72
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        94..101
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        123..132
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        133..153
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        154..167
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        189..301
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        302..322
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        323..348
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        349..369
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        370..421
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        422..442
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        443..453
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        454..474
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        475..529
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        530..550
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        551..569
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        570..590
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        591..987
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        988..1008
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        1009..1031
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1032..1052
FT                   /note="Helical; Name=13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        1053..1124
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1125..1145
FT                   /note="Helical; Name=14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        1146..1242
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1243..1263
FT                   /note="Helical; Name=15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        1264..1546
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          297..595
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          669..909
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          991..1271
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          1309..1543
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          941..964
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        947..963
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         702..709
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         1343..1350
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        9
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         636..670
FT                   /note="Missing (in isoform SUR2C)"
FT                   /evidence="ECO:0000303|PubMed:8826984"
FT                   /id="VSP_000059"
FT   VAR_SEQ         1505..1546
FT                   /note="SSIVDAGLVLVFSEGILVECDTGPNLLQHKNGLFSTLVMTNK -> HTILTA
FT                   DLVIVMKRGNILEYDTPESLLAQEDGVFASFVRADM (in isoform SUR2B)"
FT                   /evidence="ECO:0000303|PubMed:8798681"
FT                   /id="VSP_000060"
SQ   SEQUENCE   1546 AA;  174239 MW;  91EEDFA2ECD9DBC2 CRC64;
     MSLSFCGNNI SSYNIYYGVL QNPCFVDALN LVPHVFLLFI TFPILFIGWG SQSSKVQIHH
     NTWLHFPGHN LRWILTFALL FVHVCEIAEG IVSDSHRASR HLHLFMPAVM GFVATTTSIV
     YYHNIETSNF PKLLLALFLY WVMAFITKTI KLVKYWQLGW GVSDLRFCIT GVMVILNGLL
     MAVEINVIRV RRYVFFMNPQ KVKPPEDLQD LGVRFLQPFV NLLSKATYWW MNTLIISAHR
     KPIDLKAIGK LPIAMRAVTN YVCLKEAYEE QKKKAADHPN RTPSIWLAMY RAFGRPILLS
     STFRYLADLL GFAGPLCISG IVQRVNEKTN TTREMFPETL SSKEFLENAH VLAVLLFLAL
     ILQRTFLQAS YYVTIETGIN LRGALLAMIY NKILRLSTSN LSMGEMTLGQ INNLVAIETN
     QLMWFLFLCP NLWAMPVQII MGVILLYNLL GSSALVGAAV IVLLAPIQYF IATKLAEAQK
     STLDYSTERL KKTNEILKGI KLLKLYAWEH IFCKSVEETR MKELSSLKTF ALYTSLSIFM
     NAAIPIAAVL ATFVTHAYAS GNNLKPAEAF ASLSLFHILV TPLFLLSTVV RFAVKAIISV
     QKLNEFLLSD EIGEDSWRAG EGTLPFESCK KHTGVQSKPI NRKQPGRYHL DSYEQARRLR
     PAETEDIAIK VTNGYFSWGS GLATLSNIDI RIPTGQLTMI VGQVGCGKSS LLLAILGEMQ
     TLEGKVYWNN VNESEPSFEA TRSRSRYSVA YAAQKPWLLN ATVEENITFG SPFNRQRYKA
     VTDACSLQPD IDLLPFGDQT EIGERGINLS GGQRQRICVA RALYQNTNIV FLDDPFSALD
     IHLSDHLMQE GILKFLQDDK RTVVLVTHKL QYLTHADWII AMKDGSVLRE GTLKDIQTKD
     VELYEHWKTL MNRQDQELEK DMEADQTTLE RKTLRRAMYS REAKAQMEDE DEEEEEEEDE
     EDNMSTVMRL RTKMPWKTCW WYLTSGGFFL LFLMIFSKLL KHSVIVAIDY WLATWTSEYS
     INHPGKADQT FYVAGFSILC GAGIFLCLVT SLTVEWMGLT AAKNLHHNLL NKIILGPIRF
     FDTTPLGLIL NRFSADTNII DQHIPPTLES LTRSTLLCLS AIGMISYATP VFLVALAPLG
     VAFYFIQKYF RVASKDLQEL DDSTQLPLLC HFSETAEGLT TIRAFRHETR FKQRMLELTD
     TNNIAYLFLS AANRWLEVRT DYLGACIVLT ASIASISGSS NSGLVGLGLL YALTITNYLN
     WVVRNLADLE VQMGAVKKVN SFLTMESENY EGTMDPSQVP EHWPQEGEIK IHDLCVRYEN
     NLKPVLKHVK AYIKPGQKVG ICGRTGSGKS SLSLAFFRMV DIFDGKIVID GIDISKLPLH
     TLRSRLSIIL QDPILFSGSI RFNLDPECKC TDDRLWEALE IAQLKNMVKS LPGGLDATVT
     EGGENFSVGQ RQLFCLARAF VRKSSILIMD EATASIDMAT ENILQKVVMT AFADRTVVTI
     AHRVSSIVDA GLVLVFSEGI LVECDTGPNL LQHKNGLFST LVMTNK
//