STAB1_MOUSE
ID STAB1_MOUSE Reviewed; 2571 AA.
AC Q8R4Y4; Q8K0K6; Q8VC09;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Stabilin-1;
DE AltName: Full=Fasciclin, EGF-like, laminin-type EGF-like and link domain-containing scavenger receptor 1;
DE Short=FEEL-1;
DE Flags: Precursor;
GN Name=Stab1; Synonyms=Feel1;
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 {ECO:0000312|EMBL:AAL91671.2};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAL91671.2};
RC TISSUE=Liver {ECO:0000312|EMBL:AAL91671.2};
RX PubMed=11829752; DOI=10.1042/0264-6021:3620155;
RA Politz O., Gratchev A., McCourt P.A.G., Schledzewski K., Guillot P.,
RA Johansson S., Svineng G., Franke P., Kannicht C., Kzhyshkowska J.,
RA Longati P., Velten F.W., Johansson S., Goerdt S.;
RT "Stabilin-1 and -2 constitute a novel family of fasciclin-like hyaluronan
RT receptor homologues.";
RL Biochem. J. 362:155-164(2002).
RN [2]
RP PROTEIN SEQUENCE OF 560-570, 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 [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1334-2571 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2230-2571 (ISOFORM 2).
RC TISSUE=Colon {ECO:0000312|EMBL:AAH31166.1}, and
RC Liver {ECO:0000312|EMBL:AAH22136.1};
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
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: Acts as a scavenger receptor for acetylated low density
CC lipoprotein. Binds to both Gram-positive and Gram-negative bacteria and
CC may play a role in defense against bacterial infection. When inhibited
CC in endothelial tube formation assays, there is a marked decrease in
CC cell-cell interactions, suggesting a role in angiogenesis. Involved in
CC the delivery of newly synthesized CHID1/SI-CLP from the biosynthetic
CC compartment to the endosomal/lysosomal system (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CHID1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000305};
CC IsoId=Q8R4Y4-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q8R4Y4-2; Sequence=VSP_050766, VSP_050767;
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DR EMBL; AF290914; AAL91671.2; -; mRNA.
DR EMBL; BC031166; AAH31166.1; -; mRNA.
DR EMBL; BC022136; AAH22136.1; -; mRNA.
DR CCDS; CCDS26906.1; -. [Q8R4Y4-1]
DR AlphaFoldDB; Q8R4Y4; -.
DR SMR; Q8R4Y4; -.
DR STRING; 10090.ENSMUSP00000046199; -.
DR GlyGen; Q8R4Y4; 31 sites.
DR iPTMnet; Q8R4Y4; -.
DR PhosphoSitePlus; Q8R4Y4; -.
DR SwissPalm; Q8R4Y4; -.
DR jPOST; Q8R4Y4; -.
DR MaxQB; Q8R4Y4; -.
DR PaxDb; Q8R4Y4; -.
DR PRIDE; Q8R4Y4; -.
DR ProteomicsDB; 257444; -. [Q8R4Y4-1]
DR ProteomicsDB; 257445; -. [Q8R4Y4-2]
DR MGI; MGI:2178742; Stab1.
DR eggNOG; KOG1218; Eukaryota.
DR InParanoid; Q8R4Y4; -.
DR PhylomeDB; Q8R4Y4; -.
DR Reactome; R-MMU-3000497; Scavenging by Class H Receptors.
DR ChiTaRS; Stab1; mouse.
DR PRO; PR:Q8R4Y4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8R4Y4; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; ISS:UniProtKB.
DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; ISS:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0007267; P:cell-cell signaling; ISS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
DR CDD; cd00055; EGF_Lam; 1.
DR Gene3D; 2.30.180.10; -; 6.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR036378; FAS1_dom_sf.
DR InterPro; IPR000782; FAS1_domain.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR000538; Link_dom.
DR Pfam; PF12947; EGF_3; 5.
DR Pfam; PF02469; Fasciclin; 4.
DR Pfam; PF00193; Xlink; 1.
DR SMART; SM00181; EGF; 23.
DR SMART; SM00179; EGF_CA; 7.
DR SMART; SM00180; EGF_Lam; 4.
DR SMART; SM00554; FAS1; 6.
DR SMART; SM00445; LINK; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR SUPFAM; SSF82153; SSF82153; 7.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01186; EGF_2; 15.
DR PROSITE; PS50026; EGF_3; 20.
DR PROSITE; PS01248; EGF_LAM_1; 2.
DR PROSITE; PS50213; FAS1; 7.
DR PROSITE; PS01241; LINK_1; 1.
DR PROSITE; PS50963; LINK_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Glycoprotein; Inflammatory response;
KW Laminin EGF-like domain; Membrane; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..2571
FT /note="Stabilin-1"
FT /id="PRO_0000007711"
FT TOPO_DOM 26..2475
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2476..2496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2497..2571
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 111..149
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000305"
FT DOMAIN 157..194
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000305"
FT DOMAIN 196..232
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000305"
FT DOMAIN 233..272
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000305"
FT DOMAIN 357..495
FT /note="FAS1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082,
FT ECO:0000305"
FT DOMAIN 507..642
FT /note="FAS1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082,
FT ECO:0000305"
FT DOMAIN 729..769
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000305"
FT DOMAIN 819..859
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000305"
FT DOMAIN 862..904
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000305"
FT DOMAIN 905..947
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000305"
FT DOMAIN 948..987
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000305"
FT DOMAIN 989..1119
FT /note="FAS1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082,
FT ECO:0000305"
FT DOMAIN 1129..1254
FT /note="FAS1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082,
FT ECO:0000305"
FT DOMAIN 1328..1393
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000305"
FT DOMAIN 1417..1455
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000305"
FT DOMAIN 1456..1497
FT /note="EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000305"
FT DOMAIN 1498..1540
FT /note="EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000305"
FT DOMAIN 1541..1583
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000305"
FT DOMAIN 1583..1709
FT /note="FAS1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082,
FT ECO:0000305"
FT DOMAIN 1725..1865
FT /note="FAS1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082,
FT ECO:0000305"
FT DOMAIN 1966..2031
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000305"
FT DOMAIN 2056..2090
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000305"
FT DOMAIN 2091..2131
FT /note="EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000305"
FT DOMAIN 2132..2174
FT /note="EGF-like 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000305"
FT DOMAIN 2208..2301
FT /note="Link"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323,
FT ECO:0000305"
FT DOMAIN 2322..2459
FT /note="FAS1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082,
FT ECO:0000305"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 674
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 713
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 817
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1011
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1088
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1097
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1728
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 113..127
FT /evidence="ECO:0000250"
FT DISULFID 121..137
FT /evidence="ECO:0000250"
FT DISULFID 139..148
FT /evidence="ECO:0000250"
FT DISULFID 161..172
FT /evidence="ECO:0000250"
FT DISULFID 165..182
FT /evidence="ECO:0000250"
FT DISULFID 184..193
FT /evidence="ECO:0000250"
FT DISULFID 200..211
FT /evidence="ECO:0000250"
FT DISULFID 205..218
FT /evidence="ECO:0000250"
FT DISULFID 220..231
FT /evidence="ECO:0000250"
FT DISULFID 237..248
FT /evidence="ECO:0000250"
FT DISULFID 242..258
FT /evidence="ECO:0000250"
FT DISULFID 260..271
FT /evidence="ECO:0000250"
FT DISULFID 733..747
FT /evidence="ECO:0000250"
FT DISULFID 741..757
FT /evidence="ECO:0000250"
FT DISULFID 759..768
FT /evidence="ECO:0000250"
FT DISULFID 823..838
FT /evidence="ECO:0000250"
FT DISULFID 832..847
FT /evidence="ECO:0000250"
FT DISULFID 866..880
FT /evidence="ECO:0000250"
FT DISULFID 874..890
FT /evidence="ECO:0000250"
FT DISULFID 892..903
FT /evidence="ECO:0000250"
FT DISULFID 909..923
FT /evidence="ECO:0000250"
FT DISULFID 917..933
FT /evidence="ECO:0000250"
FT DISULFID 935..946
FT /evidence="ECO:0000250"
FT DISULFID 952..965
FT /evidence="ECO:0000250"
FT DISULFID 959..975
FT /evidence="ECO:0000250"
FT DISULFID 1333..1347
FT /evidence="ECO:0000250"
FT DISULFID 1341..1357
FT /evidence="ECO:0000250"
FT DISULFID 1359..1368
FT /evidence="ECO:0000250"
FT DISULFID 1380..1391
FT /evidence="ECO:0000250"
FT DISULFID 1384..1401
FT /evidence="ECO:0000250"
FT DISULFID 1403..1412
FT /evidence="ECO:0000250"
FT DISULFID 1421..1431
FT /evidence="ECO:0000250"
FT DISULFID 1425..1441
FT /evidence="ECO:0000250"
FT DISULFID 1443..1454
FT /evidence="ECO:0000250"
FT DISULFID 1460..1473
FT /evidence="ECO:0000250"
FT DISULFID 1467..1483
FT /evidence="ECO:0000250"
FT DISULFID 1485..1496
FT /evidence="ECO:0000250"
FT DISULFID 1502..1515
FT /evidence="ECO:0000250"
FT DISULFID 1509..1525
FT /evidence="ECO:0000250"
FT DISULFID 1527..1539
FT /evidence="ECO:0000250"
FT DISULFID 1545..1558
FT /evidence="ECO:0000250"
FT DISULFID 1552..1568
FT /evidence="ECO:0000250"
FT DISULFID 1570..1582
FT /evidence="ECO:0000250"
FT DISULFID 1971..1985
FT /evidence="ECO:0000250"
FT DISULFID 1979..1995
FT /evidence="ECO:0000250"
FT DISULFID 1997..2006
FT /evidence="ECO:0000250"
FT DISULFID 2018..2029
FT /evidence="ECO:0000250"
FT DISULFID 2023..2039
FT /evidence="ECO:0000250"
FT DISULFID 2041..2050
FT /evidence="ECO:0000250"
FT DISULFID 2060..2070
FT /evidence="ECO:0000250"
FT DISULFID 2064..2076
FT /evidence="ECO:0000250"
FT DISULFID 2078..2089
FT /evidence="ECO:0000250"
FT DISULFID 2095..2108
FT /evidence="ECO:0000250"
FT DISULFID 2102..2117
FT /evidence="ECO:0000250"
FT DISULFID 2119..2130
FT /evidence="ECO:0000250"
FT DISULFID 2136..2150
FT /evidence="ECO:0000250"
FT DISULFID 2144..2160
FT /evidence="ECO:0000250"
FT DISULFID 2162..2173
FT /evidence="ECO:0000250"
FT DISULFID 2230..2299
FT /evidence="ECO:0000250"
FT DISULFID 2254..2275
FT /evidence="ECO:0000250"
FT VAR_SEQ 2381..2403
FT /note="TLSGPDLELHASNATFLSINASR -> VTAGPWAVCSSAVGPTQQVLLCS
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_050766"
FT VAR_SEQ 2405..2571
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_050767"
SQ SEQUENCE 2571 AA; 276257 MW; 77D00B943DC47718 CRC64;
MAEPRTLLLL CVLVLCLSDS SFIRGQTVRS KRCDIHTKFV THTPCTACAA IRRQLCPWGW
SRNFPEKILL DCRYELQLRG AAISLSGCSQ ECWKDVVQKA CCPGYWGSQC FECPGGPATP
CSGHGTCLDG IEGNGTCVCQ GNFSGSVCQE CRDPNRFGPD CQSVCNCVHG VCSHGPRGDG
SCRCFAGYTG PHCDQELPVC QSLKCPQNSQ CSAEAPTCKC LPGYTQQDNV CLAPDPCQPS
ACSPLARCSV TPQGQAQCQC PENYHGDGKV CLPRDPCLTN FGGCPSNSTF CLYRGPGKAT
CMCRPGMTSI NNNASEGCHV SCKPHSCDRS ATCQVTPDRK TSCVCKNDEV GDGHACYGHL
LHEVRRANQN GLVFLRLRAA IAMLEQGCQE ILTTSGPFTV LVPSMFSVSS VSSNMNATLA
QQLCRQHVIA GEHMLENAGP PSTRRWWTLA GQEVTITFKN MRYAYKYEDQ PQQFSIHKAN
YIAANGVFHT VTALRWQLPP PLPGDSKKTV GQILASTEVF TRFETILENC GLPSILDGPG
PFTVFAPSNE AVDSLRDGRL IYLFTAGLSK LQELVRYHIY NHGQLTVEKL ISKGRVLTMA
NQVLTVNISE GGRILLGPGG IPVRRVDVPA ANGVIHMLEG ILLPPTILPI LPKHCDEEQH
QTVLGSCVDC QALNTSVCPP NSVKMDIFPK ECVYIHDPNG LNVLKKGCAD YCNQTITKRG
CCKGFFGPDC TQCPGGFSNP CYGKGNCSDG VRGNGACLCF PDYKGIACHI CSDPKKHGEQ
CQEDCGCVHG LCDNRPGSGG VCQQGTCAPG FQGRFCNESM GNCGSTGLAQ PCHSDAHCVI
QEGVARCVCH DGFEGNGFSC KRSNPCSRPD RGGCSENAEC VPGDLGTHHC ICHKGWSGDG
RICVAIDECG LDTRGGCHAD ALCSYVGPGQ SRCTCKLGFA GNGYECSPID PCRVGNGGCH
GLATCKAVGG GQRVCTCPPH FGGDGFSCYG DIIQELEANA HFSAFSQWFK NSSITLPADS
RVTALVPSES AIRRLSLEDQ AFWLQPKMLP ELARAHFLQG AFSEEELARL NGQQVATLSA
TTRWQIHNIS GKVWVQNATV DVPDLLATNG ILHIVSQVLL PPRGDMQTGP GLLQQLDSVP
AFRLFGEQLK HHKLVAQIEA AKAYTIFVPT NHSLETQGNN SVLGIDTVRH HVILGEALSV
EVLRKGGHRN SLLGPAHWLV FYNHSGQPEV NHMPLEGPLL EAPGSSLFGL SGILAVGSSR
CLHSHAEALR EKCINCTRKF RCTQGFQLQD TPRKSCVYRS GLSFSRGCSY TCAKKIQVPD
CCPGFFGTLC EPCPGGLGGV CSGHGQCQDR FLGNGECRCQ EGFHGTACEM CELGRYGPTC
SGVCDCDHGL CQEGLRGNGS CVCHAGWQGL RCDQKITDHQ CPKKCDPNAN CIQDSAGIPA
CVCAAGYSGN GSYCSEVDPC ASGHGGCSPY ANCTKVAPGQ RTCTCQDGYT GDGELCQEIN
SCLVHNGGCH VHAECIPTGP QQVSCSCREG YSGDGIQTCK LLDPCSQNNG GCSPYAVCKS
TGDGQRTCSC DATHTVGDGI TCHGRVGLEL LRNKYASFFS LHLLEYKELK GDGPFTVFVP
HADLISNMSQ DELARIRAHR QLVFRYHVVG CRKLWSQEML DQGYITTLSG HTLRVSEREG
SIYLNDFARV VSSDLEVVNG VLHFIDHVLL PPDVLHWESG AIPIPQRNVT AAAESFGYKI
FSRLLTVAGL LPMLQDASHR PFTMLWPTDS ALQALPPDRK NWLFHEDHRD KLAAILRGHM
IRNIEALASD LPNLGQLRTM HGNTISFSCG LTRPGELIVG EDEAHIVQRH LTFEGGLAYG
IDQLLEPPDL GARCDRFEPQ PLQMKTCSIC GLEPPCPRGS REQGSPETCW RHYSKFWTTP
LHSISMRGAY WIPSSFWNRN HMSRGCHRNC VTTVWKPSCC PGHYGINCHA CPGGPRSPCS
DHGVCLDGIR GSGQCNCHPG FAGTACELCA PGAFGPQCQA CRCTQHGRCD EGLGGSGSCF
CDEGWTGARC EVQLELQPVC TPPCAPQAVC RLGNSCECSL GYEGDGRVCT VADLCQKGHG
GCSKHANCSQ VGTVVTCTCL PDYEGDGWSC RARDPCLDGH RGGCSEHADC LNTGPNTRRC
ECHVGYVGDG LQCLEELEPP VDRCLGGSSP CHTDALCTDL HFQEKQAGVF HIQATSGPYG
LTFSEAKEAC EGQGAVLASL PQLSAAQQLG FHVCFVGWLA NGSAAHPVVT PAADCGNNRV
GVVSLGVRKN LSELWDAYCY RVQDVACQCR AGFVGDGIST CNGKLLDVLA ATANFSTFYG
MLLGYANATQ RGLEFMDFLE DELTYKTLFV PVNKGFVDNM TLSGPDLELH ASNATFLSIN
ASRGTLLPAH SGLSLFISDT GPDNTSLVPL APGAVVVSHV IVWDIMAFNG IIHALASPLL
MPPQTRAVLG SEPPPVALSL GVVVTSGTLL GLVAGALYLR ARGKPPGFSF SAFQAEDNAD
DDFSPWQEGT SPTLVSVPNP VFGSSDIFCE PFDDSVLEED FPDTQRVLKV K
