CUBN_CANLF
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 03-AUG-2022, entry version 126.
DE RecName: Full=Cubilin;
DE Flags: Precursor;
GN Name=CUBN;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 34-46; 67-81; 113-120;
RP 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).
RN [2]
RP INTERACTION WITH AMN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP GLYCOSYLATION.
RX PubMed=15845892; DOI=10.1182/blood-2005-03-1197;
RA He Q., Madsen M., Kilkenney A., Gregory B., Christensen E.I., Vorum H.,
RA Hoejrup P., Schaeffer A.A., Kirkness E.F., Tanner S.M., de la Chapelle A.,
RA Giger U., Moestrup S.K., Fyfe J.C.;
RT "Amnionless function is required for cubilin brush-border expression and
RT intrinsic factor-cobalamin (vitamin B12) absorption in vivo.";
RL Blood 106:1447-1453(2005).
CC -!- FUNCTION: Endocytic receptor which plays a role in lipoprotein, vitamin
CC and iron metabolism by facilitating their uptake. Acts together with
CC LRP2 to mediate endocytosis of high-density lipoproteins, GC,
CC hemoglobin, ALB, TF and SCGB1A1. Acts together with AMN to mediate
CC endocytosis of the CBLIF-cobalamin complex. Binds to ALB, MB, Kappa and
CC lambda-light chains, TF, hemoglobin, GC, SCGB1A1, APOA1, high density
CC lipoprotein, and the CBLIF-cobalamin complex. Ligand binding requires
CC calcium. Serves as important transporter in several absorptive
CC epithelia, including intestine, renal proximal tubules and embryonic
CC yolk sac. May play an important role in the development of the peri-
CC implantation embryo through internalization of APOA1 and cholesterol.
CC Binds to LGALS3 at the maternal-fetal interface.
CC {ECO:0000250|UniProtKB:O60494}.
CC -!- SUBUNIT: Interacts with AMN (PubMed:15845892). Component of the cubam
CC complex composed of one CUBN trimer and one AMN chain (By similarity).
CC The cubam complex can dimerize (By similarity). Interacts with LRP2 in
CC a dual-receptor complex in a calcium-dependent manner. Found in a
CC complex with PID1/PCLI1, LRP1 and CUBNI. Interacts with LRP1 and
CC PID1/PCLI1 (By similarity). {ECO:0000250|UniProtKB:F1RWC3,
CC ECO:0000250|UniProtKB:O60494, ECO:0000269|PubMed:15845892}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:Q9JLB4}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O60494}. Cell membrane
CC {ECO:0000269|PubMed:15845892}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O60494}. Membrane, coated pit
CC {ECO:0000250|UniProtKB:O60494}. Endosome
CC {ECO:0000250|UniProtKB:O60494}. Lysosome membrane
CC {ECO:0000250|UniProtKB:O70244}; Peripheral membrane protein
CC {ECO:0000305}. Note=Lacks a transmembrane domain and depends on
CC interaction with AMN for location at the plasma membrane
CC (PubMed:15845892). Colocalizes with AMN and LRP2 in the endocytotic
CC apparatus of epithelial cells (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:O70244, ECO:0000269|PubMed:15845892}.
CC -!- TISSUE SPECIFICITY: Detected in kidney cortex (at protein level).
CC Detected in kidney, duodenum and jejunum.
CC {ECO:0000269|PubMed:15845892}.
CC -!- DOMAIN: The CUB domains 5 to 8 mediate binding to CBLIF and ALB. CUB
CC domains 1 and 2 mediate interaction with LRP2.
CC {ECO:0000250|UniProtKB:O70244}.
CC -!- DOMAIN: The cubam complex is composed of a 400 Angstrom long stem and a
CC globular crown region. The stem region is probably formed by AMN and
CC the CUBN N-terminal region, including the EGF-like domains. The crown
CC is probably formed by the CUBN CUB domains.
CC {ECO:0000250|UniProtKB:F1RWC3}.
CC -!- PTM: The precursor is cleaved by a trans-Golgi proteinase furin,
CC removing a propeptide. {ECO:0000250|UniProtKB:O60494}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15845892}.
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DR EMBL; AF137068; AAF14258.1; -; mRNA.
DR RefSeq; NP_001003148.1; NM_001003148.1.
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; KOG4292; Eukaryota.
DR InParanoid; Q9TU53; -.
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:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0038024; F:cargo receptor activity; IEA:InterPro.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
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; IPR028876; Cubilin.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
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 PANTHER; PTHR45656:SF11; PTHR45656:SF11; 3.
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; Cell membrane; Cholesterol metabolism;
KW Cleavage on pair of basic residues; Coated pit; Cobalamin; Cobalt;
KW Direct protein sequencing; Disulfide bond; EGF-like domain; Endosome;
KW Glycoprotein; Lipid metabolism; Lysosome; Membrane; Metal-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Signal;
KW Steroid metabolism; Sterol metabolism; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..32
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:O60494"
FT /id="PRO_0000046070"
FT CHAIN 33..3620
FT /note="Cubilin"
FT /id="PRO_0000046071"
FT DOMAIN 129..165
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 167..208
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 260..301
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 302..345
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 346..382
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 392..427
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 429..465
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 471..583
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 587..699
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 705..812
FT /note="CUB 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 813..924
FT /note="CUB 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 928..1038
FT /note="CUB 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 1044..1158
FT /note="CUB 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 1162..1274
FT /note="CUB 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 1275..1386
FT /note="CUB 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 1388..1503
FT /note="CUB 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 1507..1616
FT /note="CUB 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 1617..1731
FT /note="CUB 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 1735..1847
FT /note="CUB 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 1849..1960
FT /note="CUB 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 1975..2088
FT /note="CUB 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 2089..2210
FT /note="CUB 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 2214..2331
FT /note="CUB 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 2333..2445
FT /note="CUB 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 2449..2562
FT /note="CUB 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 2567..2684
FT /note="CUB 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 2686..2798
FT /note="CUB 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 2802..2916
FT /note="CUB 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 2917..3032
FT /note="CUB 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 3034..3147
FT /note="CUB 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 3154..3271
FT /note="CUB 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 3275..3392
FT /note="CUB 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 3392..3504
FT /note="CUB 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 3508..3620
FT /note="CUB 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT REGION 39..46
FT /note="Interaction with AMN"
FT /evidence="ECO:0000250|UniProtKB:O60494"
FT BINDING 976
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O60494"
FT BINDING 984
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O60494"
FT BINDING 1023
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O60494"
FT BINDING 1025
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O60494"
FT BINDING 1026
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O60494"
FT BINDING 1092
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O60494"
FT BINDING 1102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O60494"
FT BINDING 1143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O60494"
FT BINDING 1210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O60494"
FT BINDING 1218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O60494"
FT BINDING 1259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O60494"
FT BINDING 1262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O60494"
FT BINDING 1325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:O60494"
FT BINDING 1333
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:O60494"
FT BINDING 1370
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:O60494"
FT BINDING 1372
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:O60494"
FT SITE 32..33
FT /note="Cleavage; by furin"
FT /evidence="ECO:0000255"
FT MOD_RES 3005
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O70244"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 708
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 745
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 777
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 853
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 953
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 980
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1643
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1799
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1816
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1882
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1961
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2082
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2589
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2810
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2920
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2942
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2986
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3039
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 133..144
FT /evidence="ECO:0000250"
FT DISULFID 138..153
FT /evidence="ECO:0000250"
FT DISULFID 155..164
FT /evidence="ECO:0000250"
FT DISULFID 171..187
FT /evidence="ECO:0000250"
FT DISULFID 181..196
FT /evidence="ECO:0000250"
FT DISULFID 198..207
FT /evidence="ECO:0000250"
FT DISULFID 264..277
FT /evidence="ECO:0000250"
FT DISULFID 271..286
FT /evidence="ECO:0000250"
FT DISULFID 289..300
FT /evidence="ECO:0000250"
FT DISULFID 306..321
FT /evidence="ECO:0000250"
FT DISULFID 313..330
FT /evidence="ECO:0000250"
FT DISULFID 333..344
FT /evidence="ECO:0000250"
FT DISULFID 350..363
FT /evidence="ECO:0000250"
FT DISULFID 357..373
FT /evidence="ECO:0000250"
FT DISULFID 396..406
FT /evidence="ECO:0000250"
FT DISULFID 401..415
FT /evidence="ECO:0000250"
FT DISULFID 417..426
FT /evidence="ECO:0000250"
FT DISULFID 433..444
FT /evidence="ECO:0000250"
FT DISULFID 438..453
FT /evidence="ECO:0000250"
FT DISULFID 455..464
FT /evidence="ECO:0000250"
FT DISULFID 471..497
FT /evidence="ECO:0000250"
FT DISULFID 524..546
FT /evidence="ECO:0000250"
FT DISULFID 587..613
FT /evidence="ECO:0000250"
FT DISULFID 640..662
FT /evidence="ECO:0000250"
FT DISULFID 705..730
FT /evidence="ECO:0000250"
FT DISULFID 757..775
FT /evidence="ECO:0000250"
FT DISULFID 813..838
FT /evidence="ECO:0000250"
FT DISULFID 865..887
FT /evidence="ECO:0000250"
FT DISULFID 928..954
FT /evidence="ECO:0000250"
FT DISULFID 981..1001
FT /evidence="ECO:0000250"
FT DISULFID 1044..1070
FT /evidence="ECO:0000250"
FT DISULFID 1099..1121
FT /evidence="ECO:0000250"
FT DISULFID 1162..1188
FT /evidence="ECO:0000250"
FT DISULFID 1215..1237
FT /evidence="ECO:0000250"
FT DISULFID 1275..1303
FT /evidence="ECO:0000250"
FT DISULFID 1330..1348
FT /evidence="ECO:0000250"
FT DISULFID 1388..1414
FT /evidence="ECO:0000250"
FT DISULFID 1441..1463
FT /evidence="ECO:0000250"
FT DISULFID 1507..1533
FT /evidence="ECO:0000250"
FT DISULFID 1560..1578
FT /evidence="ECO:0000250"
FT DISULFID 1617..1644
FT /evidence="ECO:0000250"
FT DISULFID 1672..1694
FT /evidence="ECO:0000250"
FT DISULFID 1735..1761
FT /evidence="ECO:0000250"
FT DISULFID 1788..1809
FT /evidence="ECO:0000250"
FT DISULFID 1902..1924
FT /evidence="ECO:0000250"
FT DISULFID 1975..2003
FT /evidence="ECO:0000250"
FT DISULFID 2029..2051
FT /evidence="ECO:0000250"
FT DISULFID 2089..2115
FT /evidence="ECO:0000250"
FT DISULFID 2214..2244
FT /evidence="ECO:0000250"
FT DISULFID 2272..2294
FT /evidence="ECO:0000250"
FT DISULFID 2333..2360
FT /evidence="ECO:0000250"
FT DISULFID 2387..2408
FT /evidence="ECO:0000250"
FT DISULFID 2449..2475
FT /evidence="ECO:0000250"
FT DISULFID 2502..2524
FT /evidence="ECO:0000250"
FT DISULFID 2567..2596
FT /evidence="ECO:0000250"
FT DISULFID 2625..2646
FT /evidence="ECO:0000250"
FT DISULFID 2686..2712
FT /evidence="ECO:0000250"
FT DISULFID 2739..2761
FT /evidence="ECO:0000250"
FT DISULFID 2802..2828
FT /evidence="ECO:0000250"
FT DISULFID 2857..2880
FT /evidence="ECO:0000250"
FT DISULFID 2917..2943
FT /evidence="ECO:0000250"
FT DISULFID 2974..2996
FT /evidence="ECO:0000250"
FT DISULFID 3034..3061
FT /evidence="ECO:0000250"
FT DISULFID 3088..3110
FT /evidence="ECO:0000250"
FT DISULFID 3154..3182
FT /evidence="ECO:0000250"
FT DISULFID 3212..3234
FT /evidence="ECO:0000250"
FT DISULFID 3275..3303
FT /evidence="ECO:0000250"
FT DISULFID 3329..3351
FT /evidence="ECO:0000250"
FT DISULFID 3392..3418
FT /evidence="ECO:0000250"
FT DISULFID 3445..3467
FT /evidence="ECO:0000250"
FT DISULFID 3508..3534
FT /evidence="ECO:0000250"
FT DISULFID 3561..3583
FT /evidence="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
