GenomeNet

Database: UniProt
Entry: Q9TU53
LinkDB: Q9TU53
Original site: Q9TU53 
ID   CUBN_CANLF              Reviewed;        3620 AA.
AC   Q9TU53;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   10-APR-2019, entry version 113.
DE   RecName: Full=Cubilin;
DE   Flags: Precursor;
GN   Name=CUBN;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 34-46; 67-81;
RP   113-120; 826-836; 2337-2351 AND 2634-2644.
RC   TISSUE=Kidney;
RX   PubMed=10552972;
RA   Xu D., Kozyraki R., Newman T.C., Fyfe J.C.;
RT   "Genetic evidence of an accessory activity required specifically for
RT   cubilin brush-border expression and intrinsic factor-cobalamin
RT   absorption.";
RL   Blood 94:3604-3606(1999).
CC   -!- FUNCTION: Cotransporter which plays a role in lipoprotein, vitamin
CC       and iron metabolism, by facilitating their uptake. Binds to ALB,
CC       MB, Kappa and lambda-light chains, TF, hemoglobin, GC, SCGB1A1,
CC       APOA1, high density lipoprotein, and the CBLIF-cobalamin complex.
CC       The binding of all ligands requires calcium. Serves as important
CC       transporter in several absorptive epithelia, including intestine,
CC       renal proximal tubules and embryonic yolk sac. Interaction with
CC       LRP2 mediates its trafficking throughout vesicles and facilitates
CC       the uptake of specific ligands like GC, hemoglobin, ALB, TF and
CC       SCGB1A1. Interaction with AMN controls its trafficking to the
CC       plasma membrane and facilitates endocytosis of ligands. May play
CC       an important role in the development of the peri-implantation
CC       embryo through internalization of APOA1 and cholesterol. Binds to
CC       LGALS3 at the maternal-fetal interface (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with LRP2 in a dual-receptor complex in a
CC       calcium-dependent manner. Component of the cubam complex composed
CC       of CUBN and AMN. The cubam complex can oligomerize and form cubam
CC       trimers. Found in a complex with PID1/PCLI1, LRP1 and CUBNI.
CC       Interacts with LRP1 and PID1/PCLI1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}. Lysosome membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Note=Colocalizes with
CC       AMN and LRP2 in the endocytotic apparatus of epithelial cells.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The CUB domains 5 to 8 mediate binding to CBLIF and ALB.
CC       CUB domains 1 and 2 mediate interaction with LRP2 (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: The precursor is cleaved by a trans-Golgi proteinase furin.
CC       The result is a propeptide cleaved off (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
DR   EMBL; AF137068; AAF14258.1; -; mRNA.
DR   RefSeq; NP_001003148.1; NM_001003148.1.
DR   UniGene; Cfa.3631; -.
DR   ProteinModelPortal; Q9TU53; -.
DR   SMR; Q9TU53; -.
DR   STRING; 9612.ENSCAFP00000006833; -.
DR   PaxDb; Q9TU53; -.
DR   PRIDE; Q9TU53; -.
DR   GeneID; 403767; -.
DR   KEGG; cfa:403767; -.
DR   CTD; 8029; -.
DR   eggNOG; KOG3714; Eukaryota.
DR   eggNOG; ENOG410ZPX7; LUCA.
DR   HOGENOM; HOG000049236; -.
DR   HOVERGEN; HBG080357; -.
DR   InParanoid; Q9TU53; -.
DR   KO; K14616; -.
DR   OrthoDB; 4105at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:CACAO.
DR   GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0008144; F:drug binding; ISS:UniProtKB.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd00041; CUB; 27.
DR   Gene3D; 2.60.120.290; -; 27.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR024731; EGF_dom.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   Pfam; PF00431; CUB; 27.
DR   Pfam; PF00008; EGF; 3.
DR   Pfam; PF12947; EGF_3; 1.
DR   Pfam; PF07645; EGF_CA; 3.
DR   SMART; SM00042; CUB; 27.
DR   SMART; SM00181; EGF; 8.
DR   SMART; SM00179; EGF_CA; 7.
DR   SUPFAM; SSF49854; SSF49854; 27.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS01180; CUB; 27.
DR   PROSITE; PS00022; EGF_1; 4.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 7.
DR   PROSITE; PS01187; EGF_CA; 4.
PE   1: Evidence at protein level;
KW   Calcium; Cholesterol metabolism; Cleavage on pair of basic residues;
KW   Cobalamin; Cobalt; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; EGF-like domain; Endosome; Glycoprotein;
KW   Lipid metabolism; Lysosome; Membrane; Metal-binding; Phosphoprotein;
KW   Protein transport; Reference proteome; Repeat; Signal;
KW   Steroid metabolism; Sterol metabolism; Transport.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   PROPEP       21     32       Removed in mature form. {ECO:0000250}.
FT                                /FTId=PRO_0000046070.
FT   CHAIN        33   3620       Cubilin.
FT                                /FTId=PRO_0000046071.
FT   DOMAIN      129    165       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      167    208       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      260    301       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      302    345       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      346    382       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      392    427       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      429    465       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      471    583       CUB 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      587    699       CUB 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      705    812       CUB 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      813    924       CUB 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      928   1038       CUB 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     1044   1158       CUB 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     1162   1274       CUB 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     1275   1386       CUB 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     1388   1503       CUB 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     1507   1616       CUB 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     1617   1731       CUB 11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     1735   1847       CUB 12. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     1849   1960       CUB 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     1975   2088       CUB 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     2089   2210       CUB 15. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     2214   2331       CUB 16. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     2333   2445       CUB 17. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     2449   2562       CUB 18. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     2567   2684       CUB 19. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     2686   2798       CUB 20. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     2802   2916       CUB 21. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     2917   3032       CUB 22. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     3034   3147       CUB 23. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     3154   3271       CUB 24. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     3275   3392       CUB 25. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     3392   3504       CUB 26. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     3508   3620       CUB 27. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   METAL       976    976       Calcium 1. {ECO:0000250}.
FT   METAL       984    984       Calcium 1. {ECO:0000250}.
FT   METAL      1023   1023       Calcium 1. {ECO:0000250}.
FT   METAL      1025   1025       Calcium 1. {ECO:0000250}.
FT   METAL      1026   1026       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL      1092   1092       Calcium 2. {ECO:0000250}.
FT   METAL      1102   1102       Calcium 2. {ECO:0000250}.
FT   METAL      1143   1143       Calcium 2. {ECO:0000250}.
FT   METAL      1210   1210       Calcium 3. {ECO:0000250}.
FT   METAL      1218   1218       Calcium 3. {ECO:0000250}.
FT   METAL      1259   1259       Calcium 3. {ECO:0000250}.
FT   METAL      1262   1262       Calcium 3; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL      1325   1325       Calcium 4. {ECO:0000250}.
FT   METAL      1333   1333       Calcium 4. {ECO:0000250}.
FT   METAL      1370   1370       Calcium 4. {ECO:0000250}.
FT   METAL      1372   1372       Calcium 4; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   SITE         32     33       Cleavage; by furin. {ECO:0000255}.
FT   MOD_RES    3005   3005       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O70244}.
FT   CARBOHYD    102    102       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    253    253       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    425    425       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    708    708       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    745    745       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    777    777       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    853    853       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    953    953       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    980    980       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1165   1165       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1214   1214       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1304   1304       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1316   1316       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1329   1329       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1497   1497       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1548   1548       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1643   1643       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1799   1799       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1816   1816       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1882   1882       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1961   1961       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2082   2082       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2114   2114       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2317   2317       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2383   2383       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2397   2397       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2528   2528       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2578   2578       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2589   2589       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2607   2607       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2810   2810       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2920   2920       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2942   2942       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2986   2986       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3039   3039       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3100   3100       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3122   3122       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3265   3265       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3280   3280       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3292   3292       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3354   3354       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3427   3427       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3454   3454       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3530   3530       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    133    144       {ECO:0000250}.
FT   DISULFID    138    153       {ECO:0000250}.
FT   DISULFID    155    164       {ECO:0000250}.
FT   DISULFID    171    187       {ECO:0000250}.
FT   DISULFID    181    196       {ECO:0000250}.
FT   DISULFID    198    207       {ECO:0000250}.
FT   DISULFID    264    277       {ECO:0000250}.
FT   DISULFID    271    286       {ECO:0000250}.
FT   DISULFID    289    300       {ECO:0000250}.
FT   DISULFID    306    321       {ECO:0000250}.
FT   DISULFID    313    330       {ECO:0000250}.
FT   DISULFID    333    344       {ECO:0000250}.
FT   DISULFID    350    363       {ECO:0000250}.
FT   DISULFID    357    373       {ECO:0000250}.
FT   DISULFID    396    406       {ECO:0000250}.
FT   DISULFID    401    415       {ECO:0000250}.
FT   DISULFID    417    426       {ECO:0000250}.
FT   DISULFID    433    444       {ECO:0000250}.
FT   DISULFID    438    453       {ECO:0000250}.
FT   DISULFID    455    464       {ECO:0000250}.
FT   DISULFID    471    497       {ECO:0000250}.
FT   DISULFID    524    546       {ECO:0000250}.
FT   DISULFID    587    613       {ECO:0000250}.
FT   DISULFID    640    662       {ECO:0000250}.
FT   DISULFID    705    730       {ECO:0000250}.
FT   DISULFID    757    775       {ECO:0000250}.
FT   DISULFID    813    838       {ECO:0000250}.
FT   DISULFID    865    887       {ECO:0000250}.
FT   DISULFID    928    954       {ECO:0000250}.
FT   DISULFID    981   1001       {ECO:0000250}.
FT   DISULFID   1044   1070       {ECO:0000250}.
FT   DISULFID   1099   1121       {ECO:0000250}.
FT   DISULFID   1162   1188       {ECO:0000250}.
FT   DISULFID   1215   1237       {ECO:0000250}.
FT   DISULFID   1275   1303       {ECO:0000250}.
FT   DISULFID   1330   1348       {ECO:0000250}.
FT   DISULFID   1388   1414       {ECO:0000250}.
FT   DISULFID   1441   1463       {ECO:0000250}.
FT   DISULFID   1507   1533       {ECO:0000250}.
FT   DISULFID   1560   1578       {ECO:0000250}.
FT   DISULFID   1617   1644       {ECO:0000250}.
FT   DISULFID   1672   1694       {ECO:0000250}.
FT   DISULFID   1735   1761       {ECO:0000250}.
FT   DISULFID   1788   1809       {ECO:0000250}.
FT   DISULFID   1902   1924       {ECO:0000250}.
FT   DISULFID   1975   2003       {ECO:0000250}.
FT   DISULFID   2029   2051       {ECO:0000250}.
FT   DISULFID   2089   2115       {ECO:0000250}.
FT   DISULFID   2214   2244       {ECO:0000250}.
FT   DISULFID   2272   2294       {ECO:0000250}.
FT   DISULFID   2333   2360       {ECO:0000250}.
FT   DISULFID   2387   2408       {ECO:0000250}.
FT   DISULFID   2449   2475       {ECO:0000250}.
FT   DISULFID   2502   2524       {ECO:0000250}.
FT   DISULFID   2567   2596       {ECO:0000250}.
FT   DISULFID   2625   2646       {ECO:0000250}.
FT   DISULFID   2686   2712       {ECO:0000250}.
FT   DISULFID   2739   2761       {ECO:0000250}.
FT   DISULFID   2802   2828       {ECO:0000250}.
FT   DISULFID   2857   2880       {ECO:0000250}.
FT   DISULFID   2917   2943       {ECO:0000250}.
FT   DISULFID   2974   2996       {ECO:0000250}.
FT   DISULFID   3034   3061       {ECO:0000250}.
FT   DISULFID   3088   3110       {ECO:0000250}.
FT   DISULFID   3154   3182       {ECO:0000250}.
FT   DISULFID   3212   3234       {ECO:0000250}.
FT   DISULFID   3275   3303       {ECO:0000250}.
FT   DISULFID   3329   3351       {ECO:0000250}.
FT   DISULFID   3392   3418       {ECO:0000250}.
FT   DISULFID   3445   3467       {ECO:0000250}.
FT   DISULFID   3508   3534       {ECO:0000250}.
FT   DISULFID   3561   3583       {ECO:0000250}.
SQ   SEQUENCE   3620 AA;  397435 MW;  00B041EE6AD07348 CRC64;
     MSSPFLWSLI ILLTFAESNG EAGGFELQRQ KRSIDFQQPR MATERGNLVF LVGSAQNIEF
     RTGSLGKIKL NEEDLGECLH QIQKNKEDIT DLKRSAVNVP QNISSQIHQL NSKLVDLERK
     FQSLQQTVDK KVCSSNPCQN GGTCLNLHDS FFCICPSQWK GPLCSVDVNE CQIYSGTPLG
     CQNGATCENT AGSYSCLCSP ETHGPQCASK YDDCEGGSKA LCVHGICEDL VRVKADEPKY
     NCICDAGWTS PLNSSACVLD IDECNLQHAP CSPLVQCFNT QGSFYCGACP TGWQGNGYSC
     QDIDECKINN GGCSVVPPVM CVNTLGSYHC QACPPGYQGD GRVCTVIDIC SVNNGGCHPE
     ASCSSVLGSL PLCTCLPGYT GNGYGPNGCA QLSDTCLSHP CLNGQCIETV SGYLCKCESG
     WAGINCTENI NECLSNPCFN GGTCVDGVNA FSCECTRFWT GFLCQIPQQV CGGSLSGMDG
     SFSYMSPDVG YVHDVNCFWV IRTEDRKVLR ITFTFFQLES VNNCPHEFLQ IHDGDSSAAL
     QLGRFCGSVL PHELLSSNNA LYFHLYSEHF RSGRGFTIRW ETQQPECGGI LMGTYGSIKS
     PGYPGNYPPG RDCVWQVVTS PDLLITFTFG TLSLEHHDDC SKDYLEIRDG PLYQDPSLGK
     FCTTLSVPPL QTTGPFARVH FHSDNQINDQ GFHITYLTSP SDLHCGGNYT DPEGLLSSDL
     SGPFTHNRQC IYIIKQPLGE QIQVNFTHVE LEGQSSCSQS HIEVRDDKIL LGKVCDNETL
     PHIKSIRNHI WIRLKIDASL VRASFRAVYQ VACGGELTGE GVIRSPFYPN VYPGERICRW
     TIHQPQSQVV ILNFTAFGIE SSAHCDTDYI EIGSSSILGS PENKKYCGTD IPLFITSVYN
     FLYVIFVKSS STENHGFMAK FSAADLACGE ILTESTGIIQ SPGHPNIYPH GINCTWHILV
     QPGHLIHLIF RKFHLEFHYN CTNDYLEVYD TGSNTYLGRY CGKSIPPSLT SSTNSLKLIF
     VADSDLAYEG FLINYEATDA SSACMEDYTE NSGTFTSPNF PNNYPNNWKC IYRITVETSQ
     QIALHFTNFA LEEAIGGQCV ADFVEIRDGG YETSPPLGTY CGSIPPPRII SHSNKLWLQF
     TSDFLGSGPG FSAYWDGSLT GCGGNITTPT GVFTSPSYPM PYYHSSECYW LLKASHGSPF
     ELEFEDFHLE HHPNCTLDYL AVYDGPSTSS HLLSQLCGNE KPPVIRSTGD SMFLKFRTDE
     DQQGGGFLAK YQQTCRNVVI VNRNYGILES IHYPNPYSDN QRCNWTIQAT TGNTVNYTFL
     AFELENHINC STDYLELYDG PRRMGRYCGA DMPPTGSTTG SKLQVLFYTD GVGHQEKGFQ
     MQWFIHGCGG ELSGTTGSFS SPGYPNTYPP NKECIWYITT APGSSIQLTI HDFDVEYHAR
     CNFDVLEVYG GPDFHSPRIT QLCSQRSSEN PMQVSSTGNE LAIRFKTDSS INGRGFNASW
     QAVPGGCGGI FQAPNGEIHS PNYPSPYRGN TDCSWVIRVE RNHRILLNFT DFDLEPQDSC
     ITAYDGLSST TTRLASVCGR QQLTNPITSS GNSLFLRFQS GPSRQGRGFR AQFNQVCGGH
     ILTNSFDTIS SPLFPAKYPN NQNCSWVIQA QPPFNHITLS FDHFGLESST TCTQDFLEIL
     DGDYDDAPLR GRYCGHSMPH PITSFSSALT LRFVSDSRVN SDGFHATYAA SSSACGGTFH
     MAEGIFNSPG YPEVYPSNVE CVWNIVSSPG NRLQLSFITF QLEDSQDCSR DFVEVREGNA
     TGHLVGRYCG NVLPLNYSSI VGHILWIRFV SDGSGSGTGF QATFTKIFGN DNIVGTHGKI
     ASPLWPGRYP HNSNYQWIVN VNATQVIHGR ILEIDIEGAQ SCYYDKLRVY DGLGIHSRLI
     GTYCGTQTTS FSSSRNSLTF QFSSDSSITG KGFLLEWFAV NASGGPLPTI ATGACGGFLR
     TGDAPVFLFS PGWPESYSNS ADCTWLIQAP DSTVELNILS LDIEAQRTCD YDKLVIRDGD
     SNLAPQLAVL CGREIPGPIR STGEYMFIRF TSDFSITGAG FNASFHKSCG GYLHADRGII
     TSPQYPETYS PNLNCSWHVL VQSGLTIAVH FEQPFQIPSG DSSCSQGDYL VLKNGPDIYS
     PPLGPYGRNG HFCGSRPSST LFTSDNQMFV QFISDGSNGG QGFKIKYEAK SLACGGNIYI
     HDVNSAGYVT SPGHPNNYPQ HADCNWLIAA PPGKLIRVQF EDQFNIEETP NCVSNYLELR
     DGVDSNAPLL AKLCGRSLPS SQLSSGEVMY LRFRSDNSST QVGFKIKYAI AQCGGRVTGQ
     SGIIESSGYP TLPYRDNSFC EWHLKGPSGH YLTIHFEDFH LQNSSGCEKD FVEIWENHTS
     GNLLGRYCGN TIPDSIDTSS NVALVRFVTD GSVTASGFRL RFESSMEACG GELQGPTGTF
     TSPNYPNPNP HGRVCEWRIM VQEGRRITLT FNNLRLEAHP SCYSEHVTIF NGIRNNSPQL
     EKLCGSVNAS SEIKSSGNTM KVVFFTDGSR PFGGFSATYT SSEDAVCGGS LTHFPEGNFT
     SPGYNGVSNY SRNLNCEWTL SNPNQGNSSI YIHFEDFYLE SHQDCQFDVL EFRVGNADGP
     LMWRLCGPSK PIVPLVIPYP EVWIHFVTNE HVEHVGFHAE YSFTDCGGIQ LGESGVIASP
     NYPASYDSLT HCSWLLEAPQ GFTITLTFSD FDIEDHATCA WDSVSVRNGG SPGSPIIGQY
     CGTSNPRTIQ SGSNQLVVIF NSDHSVQNGG FYATWNTQTL GCGGILHSDN GTIRSPHWPQ
     NFPENSRCSW TVITHESKQL EISFDNNFRI PSGDGQCQNS FVKVWAGTEE VAESLLATGC
     GNVAPGSILT PRNVFIAVFQ SQETPAQGFS ASFVSRCGGN FTNPSGYILS PNYPRQYDNN
     MNCTYIIEAD PLSVVLLTFE SFHLEARSAI TGSCANDGVH IIRGSNLSST PFATVCGNEI
     LSPVTILGPV LLNFYSNAHT TDLGFKFNYK ITSCGGVFNV STGVIKSPAY SYSDYPNNIY
     CLYTIVGRDD RVVQLKFSDF DVVPSTFCSQ DYLAIYDGSN ISDPLLGKFC GSNLPPNIKS
     SNHSMLLVFK TDSFQTARGW KITFQQTLGP QQGCGGYLTG SDNTFASPDS DSNGRYDKNL
     NCVWFIIAPV NKLIKLTFNT FALEAQSAMQ RCIYDYVKLY DGDSENANLA GTFCGSTVPA
     PFISSGNFLT VQFVSDVTLE REGFNATYTT VDMPCGGTYN ATWTPQSISS PNSSNPEVPL
     SMCMWFLEAP PHQQVKITVW ALELHSQDCD QNYLEFRDSP ESNGSPGPQI CGRNASATPT
     FYSSRSTAIV IFKSEVLNRN SRVGFTYQIA GCNREYNKAF GNLKSPGWPD NYDNNLDCTV
     ILTAPQNHTI SLFFHSFGIE DSSECTHDFL EVRNGSDSSS PLFGTYCGTL LPDPIFSRNN
     KLYLRFKTDS ATSNRGYEIV WTSSPSGCGG TLYGDSGSFT SPGYPGTYPN NTDCEWAIIA
     PAGRPVTVTF YFISIDDPGD CVQNYLILYD GPDANSPSFG PYCGADTNIA PFVASSHRVF
     IKFHAEYAVY PSAIRLTWDS
//
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