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Database: UniProt
Entry: A0A091DQL9_FUKDA
LinkDB: A0A091DQL9_FUKDA
Original site: A0A091DQL9_FUKDA 
ID   A0A091DQL9_FUKDA        Unreviewed;      4353 AA.
AC   A0A091DQL9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Basement membrane-specific heparan sulfate proteoglycan core protein {ECO:0000313|EMBL:KFO32565.1};
GN   ORFNames=H920_06126 {ECO:0000313|EMBL:KFO32565.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO32565.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO32565.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO32565.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; KN122157; KFO32565.1; -; Genomic_DNA.
DR   STRING; 885580.ENSFDAP00000004628; -.
DR   eggNOG; KOG3509; Eukaryota.
DR   Proteomes; UP000028990; Unassembled WGS sequence.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR   GO; GO:0072359; P:circulatory system development; IEA:UniProt.
DR   CDD; cd00054; EGF_CA; 4.
DR   CDD; cd00055; EGF_Lam; 8.
DR   CDD; cd00096; Ig; 6.
DR   CDD; cd05743; Ig_Perlecan_like; 1.
DR   CDD; cd05754; IgI_Perlecan_like; 1.
DR   CDD; cd00110; LamG; 3.
DR   CDD; cd00112; LDLa; 4.
DR   Gene3D; 2.60.120.200; -; 3.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 22.
DR   Gene3D; 2.10.25.10; Laminin; 10.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 4.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR002049; LE_dom.
DR   InterPro; IPR000082; SEA_dom.
DR   PANTHER; PTHR45080; CONTACTIN 5; 1.
DR   PANTHER; PTHR45080:SF32; MYOTILIN; 1.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF07679; I-set; 7.
DR   Pfam; PF13927; Ig_3; 15.
DR   Pfam; PF00052; Laminin_B; 3.
DR   Pfam; PF00053; Laminin_EGF; 9.
DR   Pfam; PF00054; Laminin_G_1; 3.
DR   Pfam; PF00057; Ldl_recept_a; 4.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 10.
DR   SMART; SM00179; EGF_CA; 5.
DR   SMART; SM00180; EGF_Lam; 9.
DR   SMART; SM00409; IG; 22.
DR   SMART; SM00408; IGc2; 22.
DR   SMART; SM00406; IGv; 8.
DR   SMART; SM00281; LamB; 3.
DR   SMART; SM00282; LamG; 3.
DR   SMART; SM00192; LDLa; 4.
DR   SMART; SM00200; SEA; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR   SUPFAM; SSF57196; EGF/Laminin; 8.
DR   SUPFAM; SSF48726; Immunoglobulin; 22.
DR   SUPFAM; SSF57424; LDL receptor-like module; 4.
DR   PROSITE; PS00022; EGF_1; 4.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS01248; EGF_LAM_1; 7.
DR   PROSITE; PS50027; EGF_LAM_2; 6.
DR   PROSITE; PS50835; IG_LIKE; 22.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 3.
DR   PROSITE; PS51115; LAMININ_IVA; 3.
DR   PROSITE; PS01209; LDLRA_1; 3.
DR   PROSITE; PS50068; LDLRA_2; 4.
DR   PROSITE; PS50024; SEA; 1.
PE   4: Predicted;
KW   Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022869};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Heparan sulfate {ECO:0000256|ARBA:ARBA00023207};
KW   Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW   ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Proteoglycan {ECO:0000256|ARBA:ARBA00023207};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          90..201
FT                   /note="SEA"
FT                   /evidence="ECO:0000259|PROSITE:PS50024"
FT   DOMAIN          417..494
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          556..692
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          726..775
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          910..1087
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          1121..1170
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1171..1227
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1237..1286
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1313..1519
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          1553..1602
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1603..1660
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1660..1754
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1760..1846
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1856..1939
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1946..2033
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2042..2123
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2136..2220
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2234..2313
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2319..2406
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2420..2502
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2509..2599
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2613..2695
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2698..2792
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2810..2892
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2904..2989
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          3005..3090
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          3095..3183
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          3194..3272
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          3281..3365
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          3382..3466
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          3469..3553
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          3558..3639
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          3645..3830
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          3828..3863
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          3866..3904
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          3910..4090
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          4086..4123
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          4125..4158
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          4183..4353
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   REGION          258..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3366..3387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          4318..4353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..279
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        229..244
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        296..308
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        303..321
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        315..330
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        336..348
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        343..361
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        355..370
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        399..414
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        745..754
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1140..1149
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1199..1208
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1211..1225
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1237..1249
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1257..1266
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1572..1581
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1631..1640
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        3853..3862
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        3875..3892
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        3894..3903
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        4113..4122
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        4148..4157
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   4353 AA;  465482 MW;  8905C1127A423825 CRC64;
     MRGTEQATTV ATGWGQPFLG ALCTEGFRLG QVTHGLRAYD GLSLPEDTEA VTAGRAGWSY
     SYLSDDEDLL ADDASGDGLG SGDLGSGDFQ MVYFRALVNF THSIEYSPQL EDAGSREFRA
     VSEAVVDRLE SEYLKTPGDQ VVSVVFIKEL DGWVFVELDV GSEGNADGAQ IQEVLYTVVS
     GGSIGSYITS PQGFQFRRLG TVPQFPRVCT ETEFACHSHN ECVALEYRCD RRPDCRDMSD
     ELDCEEPVPE VVSMPSVVQE MSPLTPRSPE ATTTRRPPDT LRPQPLLPDL ARPMLCGPHE
     AACHSGPCIP KDYLCDGQED CKDGSDELDC GPPPPCEPNE FPCGNGHCAL KLWRCDGDFD
     CEDRTDETNC PAKQPGEVCA PTQFRCISTN TCIPASFHCD EESDCPDRSD EFGCMPPQVV
     TPPQETIQAS RGQTVTFTCV AIGVPTPIIN WRLNWGHIPS HPRVTMTSEG GRGTLTIHDV
     KEADQGAYTC EAMNARGMVF GIPDGVLELI PQRGPCPDGH FYLEPSASCL PCFCFGVTNV
     CQSSRRFRDQ IQLRFDQPGD FKGVNVTSPS QPGTPPLAST QLQVDTALQE FQLVDLSRRF
     LTHDSFWALP ELFLGNKVDS YGGSLRYSEH WVHESGRPVQ RAEMLQVLQS LEAVLIQTVY
     NAKMASVGLS DVTMDTTVTH ATSHGRAHSV EECRCPIGYS GLSCESCDAH FTRVPSGPYL
     GTCSGCNCNG HSSSCDPVYG HCLNCQHNTE GPQCNKCKAG FFGDATKPTA TACRPCPCPY
     IDASRRFSDT CFLDTDGQAT CDACAPGYTG RRCESCAPGY EGNPIQPSGK CRPTNQAIVR
     CDERGSVGSA GESCLCKNNV VGRLCNECAE GSFHLSTHNP DGCLKCFCMG VSRRCTSSSW
     SRAQVLGASE EPTQFSLTNA AGTHTTSEGI SSPSSGELVF SSFHSLLSGP YFWSLPARFR
     GDKVTSYGGE LRFTVTQRPQ PSSAPLHGQP LVVLQGNGIT LEHHTSREPS PGQPSTFTVP
     FREQAWQRPD GQPATREHLL MALAGIDALL IQASHTQRPM ESRVSDLSMD VAVPEVTSQD
     PALEVEQCTC PPGYRGPSCQ DCDTGFTRMP GGLYLGTCER CSCHGHAEAC EPETGACQGC
     QHHTEGSRCE QCQPGYYGDA QRGTPQDCQL CPCHGAPAAG QAAHTCFLDT DGHPTCDSCS
     PGHSGRHCER CAPGYYGNPR LGQPCQRDGQ VPDGTGCKCD PQGSISSQCD AAGQCQCKAQ
     VQGPTCSHCQ PHHFYLSASN PEGCLPCFCM GVTQQCASSS YTRHVIYTYF APGDFQGFAL
     VNPQRNSRLA EDFTVEPVPD GAQLSFGNFA HLGHESFYWQ LPEMYQGDKF SLSYEGFSLL
     PESLYYWQLP QAFLGDKVAA YGGKLRYTLS YTAGPQGSPL SDPDVQIMGN NIMLVASQPA
     PQGPEKKSYE IVFREEFWRR PDGQPATREH LLMALADLDE LLIRATFTSV PLAASISAVS
     LEVAQRGPLD GPRALEVEEC RCPPGYMGLS CQDCAPGYTR TGSGLYLGHC ELCECNGHSD
     LCHPETGACS QCQHNAAGEF CELCAPGYYG DATAGTPEDC QPCACPLTNP ENMFSRTCES
     LGAGGYRCTA CEPGYTGQYC EQCAPGYVGN PNVQGGRCLP QTDQASLVVQ VHPARSVVPE
     GGSHSLRCQA SGNPPHYFYW SREDGQPVPS STQQRHQGAE LHFPSVQPSD AGVYLCTCRS
     LHHVNASRAE LLVTEAPSKP ITVTVEEQRS QSVRPGADVT FICTAKSKSP AYTLAWTRLH
     NGKLPSRAMD FNGILTVRNV QPSDAGTYVC TGSNMFAMDQ GTATLHVQGS STSSAPVVSI
     HPPQLTVQPG QMAEFRCSAR GNPTPTLEWI GGPGGQLPPK AQIHGGLLRL PAAEPSDQGQ
     YVCRALNSAG QHMGRAVLQV HGSNGPRVQV SPERIQVHEG HTVRLYCRAT GVPTATITWR
     KEGGSLPPQA RSERMDISTL VIPAITSADA GFYLCVATSP TGTAQARIQV AVTSASGASS
     VPVRIESSSP TVTEGQLLDL SCVAAGFAHS QITWYKRGGS LPPHAQVHGS RLRLPQVSPA
     DSGEYVCRVE SEAGAKEASI VVSVLNSAQL GLSRVPGSTQ PIHIESSSSH VAEGQTLDLN
     CVVPGQAQVT WHKRGGSLPA RHQTHGSLLR LHQVSPADSG EYVCHVVLGS KHLETSVLVS
     IKPSDSIPAP APVPPIRIES SSPTVTEGQS LDLSCMVAGQ AHAQVTWYKR GGSLPARHQV
     RGSHLYIFQV SPADAGEYVC RASSGAEASI TVTVTRTYPT GSTQPIRIES SSSHVAEGQT
     LDLNCVVPGQ AHAQVTWHKR GGSLPAQHQT HGSLLRLHQV SPADSGEYVC QVVGSPVPLE
     TSVLVSIEPV GSVPALGVTP PIRIESSSSH VAEGQTLDLN CMVQGQAQAQ ITWHKLGGNL
     PARHQVHGSR LRLPQVTPAD SGEYVCRVTS GSDTYEASVL VSIQQRLSPS QTQSVLYPIH
     IESSSASLAN GHTLDLNCLV ATHTPHTITW YKRGGSLPSR HQIVGSRLRI PQVTPADSGE
     YVCHVSNGAG SQETSLIVTI QGSGSSQVPS VSPPIRIESS SPTVVEGQTL DLNCVLAGQT
     QATITWYKRG GSLPAKHQTH GSHLQLHQLS VADSGEYVCR ANNNIDAQEA SIMVSVSPST
     HKPSAPGGAG PIQIESSSSH ITEGQTLDLN CVFPGQAHAQ VTWHRRRGSL PAHHQTHGSR
     LRLYQVSPAD SGEYVCRVLG SSGPQEASVL VTIEASGSST VRVPATGGAP PIHIEKSSSR
     VAEGQTLDLN CVVPGQAHAQ VTWHKRGGSL PAQHQVHGPL LRLNHVSPAD SGEYSCQVTG
     SSGTLEASVL VTVEASSPGP IPAPGLAQPI YIEASSSHVA EGQTVDLNCV VTGQAHAQVT
     WHKRGGSLPT QHQTHGSRLR LHHVSPADSG EYICRVAGGS GSEQEASFTV TVTPSSGSSY
     RLRSPVISID PPSSTVHQGQ DASFRCLIHE GALPISLEWK TRNQELEDNV HISPNGSIIT
     IVGTRPSNHG AYRCVASNTY GVAQSVVNLS VQGPPTVSVL PEGPVWVKAG KDITLECVSP
     GEPRSSVRWT RVGSPARIEP RTYGHVNSHA VLKISSAKPS DAGTYVCLAQ NALGTAQKRV
     EVTVDTGTAA PGAPQVQVEE AELTVEAGYT ATLRCSATGS PPPIIHWSKL RSPLPWQHRQ
     EGDTLIIPQV AQQDSGQYIC NATSPTGHAE ATILLHVESP PYATIVPEQV SVQAGKPVQL
     QCLAHGTPPL TFQWSRVGGS LPGRATTRSQ LLHLEPAGPE DAGRYRCQVT NKVGSAEAFA
     QVLIEGPSGS LPDTRGPAEP SPTVQVTPQL DTKSIGASAE FHCAVPGDRG TQLHWFKEGS
     QLPPGHSVQD GVLRLQNLDQ SYQGTYVCQA HGPWGQAQAS ARLIVQALPS VLINTRTSVQ
     TVVVGHSVEF ECLALGDPKP QVTWSKVGGR LRPGIMQSGS VIRIAHVELA DAGQYRCTAT
     NAAGTTQSHV LLLVQALPQI STPPEVRVPA GSAAVFPCMA SGYPAPNITW SKLDGDLPPG
     SRLEKNMLML PSVRPQDAGT YVCTATNRQG KVKAFAYLQV PERVVPYFTQ TPHSFLPLPT
     IKDAYRKFEI KITFRPDSAD GMLLYNGQKR GPGSPTNLAS RQPDFISFGL VGGRPEFRFD
     AGSGMATIRH PTPLALGQFH TVTLLRSLTQ GSLIVGSLAP VNGTSQGKFQ GLDLNEELYL
     GGYPDYGAIP KAGLSGGFVG CVRELCIQGE EIIFHDLNLT AHGISHCPTC RDRPCQNGGQ
     CHDSESSSYV CVCPSGFTGS RCEHSQALHC HPEACGPDAT CVNRPDGRGY TCRCHLGRSG
     MRCEEGVTVT TPSMSGTGSY LALPALTNTH HELRLDVEFK PLVPDGILLF SGGRIGPVED
     FVSLAMVGGH LEFRYELGSG LAVLRSPEPL ALGRWHRVSA ERLNKDGSLR VNGGRPVLRS
     SPGKSQGLNL HTLLYLGGVE PSVPLSPATN VSAHFRGCVG EVSVNGKRLD LTYSFLGSQG
     IGQCYDSSPC ERQPCRNGAT CMPAGEYEFQ CLCQDGFKGD LCEHEENPCQ LREPCLHGGT
     CQGTHCLCPP GFSGSHCQQG SGHGTVESDW HVEGSGGNDA PGQYGAFFQD NGFLALPSRV
     FSRSLPEVPE TIELEVRTST ASGLLLWQGM ETGETNRGKD FIGLGLQDGH LVFSYQLGSG
     EARLVSEDPV NDGEWHRVTV LREGRRGSIQ VDGEELVSGQ SPGPNVAVNT KGSVYIARDT
     PRGCKEEPPP SSSLEHPALR FHHTEPQPPL SWK
//
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