NOTC1_XENTR
ID NOTC1_XENTR Reviewed; 2522 AA.
AC A2RUV0; F7CY31;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Neurogenic locus notch homolog protein 1;
DE Short=Notch 1;
DE Contains:
DE RecName: Full=Notch 1 extracellular truncation;
DE Short=NEXT;
DE Contains:
DE RecName: Full=Notch 1 intracellular domain;
DE Short=NICD;
DE Flags: Precursor;
GN Name=notch1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND GLYCOSYLATION AT THR-231 AND THR-1400.
RX PubMed=24226769; DOI=10.1038/nature12723;
RA Boskovski M.T., Yuan S., Pedersen N.B., Goth C.K., Makova S., Clausen H.,
RA Brueckner M., Khokha M.K.;
RT "The heterotaxy gene GALNT11 glycosylates Notch to orchestrate cilia type
RT and laterality.";
RL Nature 504:456-459(2013).
CC -!- FUNCTION: Functions as a receptor for membrane-bound ligands Jagged-1
CC (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate
CC determination. Upon ligand activation through the released notch
CC intracellular domain (NICD) it forms a transcriptional activator
CC complex with RBPJ/RBPSUH and activates genes of the enhancer of split
CC locus. Affects the implementation of differentiation, proliferation and
CC apoptotic programs. Involved in angiogenesis; negatively regulates
CC endothelial cell proliferation and migration and angiogenic sprouting.
CC Involved in the maturation of both CD4(+) and CD8(+) cells in the
CC thymus. Important for follicular differentiation and possibly cell fate
CC selection within the follicle. During cerebellar development, functions
CC as a receptor for neuronal DNER and is involved in the differentiation
CC of Bergmann glia. Represses neuronal and myogenic differentiation. May
CC play an essential role in postimplantation development, probably in
CC some aspect of cell specification and/or differentiation. May be
CC involved in mesoderm development, somite formation and neurogenesis (By
CC similarity). Involved in determination of left/right symmetry by
CC modulating the balance between motile and immotile (sensory) cilia at
CC the left-right organiser (LRO). {ECO:0000250|UniProtKB:Q01705,
CC ECO:0000269|PubMed:24226769}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q01705};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q01705}.
CC -!- SUBCELLULAR LOCATION: [Notch 1 intracellular domain]: Nucleus
CC {ECO:0000250|UniProtKB:Q01705}. Note=Following proteolytical processing
CC NICD is translocated to the nucleus. {ECO:0000250|UniProtKB:Q01705}.
CC -!- PTM: O-glycosylated on the EGF-like domains. Contains both O-linked
CC fucose and O-linked glucose. O-linked glycosylation by galnt11 is
CC involved in determination of left/right symmetry: glycosylation
CC promotes activation of notch1, possibly by promoting cleavage by
CC adam17, modulating the balance between motile and immotile (sensory)
CC cilia at the left-right organiser (LRO). {ECO:0000269|PubMed:24226769}.
CC -!- PTM: Synthesized in the endoplasmic reticulum as an inactive form which
CC is proteolytically cleaved by a furin-like convertase in the trans-
CC Golgi network before it reaches the plasma membrane to yield an active,
CC ligand-accessible form. Cleavage results in a C-terminal fragment N(TM)
CC and a N-terminal fragment N(EC). Following ligand binding, it is
CC cleaved by adam17 to yield a membrane-associated intermediate fragment
CC called notch extracellular truncation (NEXT). Following endocytosis,
CC this fragment is then cleaved by presenilin dependent gamma-secretase
CC to release a Notch-derived peptide containing the intracellular domain
CC (NICD) from the membrane (By similarity).
CC {ECO:0000250|UniProtKB:Q01705}.
CC -!- SIMILARITY: Belongs to the NOTCH family. {ECO:0000305}.
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DR EMBL; AAMC01043423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01043424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01043425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01043426; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC133053; AAI33054.1; -; mRNA.
DR RefSeq; NP_001090757.1; NM_001097288.1.
DR AlphaFoldDB; A2RUV0; -.
DR SMR; A2RUV0; -.
DR STRING; 8364.ENSXETP00000053343; -.
DR PaxDb; A2RUV0; -.
DR GeneID; 100037842; -.
DR KEGG; xtr:100037842; -.
DR CTD; 4851; -.
DR Xenbase; XB-GENE-479318; notch1.
DR eggNOG; KOG1217; Eukaryota.
DR OrthoDB; 7525at2759; -.
DR TreeFam; TF351641; -.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005112; F:Notch binding; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0061314; P:Notch signaling involved in heart development; IMP:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IBA:GO_Central.
DR GO; GO:0050793; P:regulation of developmental process; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR008297; Notch.
DR InterPro; IPR035993; Notch-like_dom_sf.
DR InterPro; IPR022362; Notch_1.
DR InterPro; IPR024600; Notch_C.
DR InterPro; IPR000800; Notch_dom.
DR InterPro; IPR010660; Notch_NOD_dom.
DR InterPro; IPR011656; Notch_NODP_dom.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00008; EGF; 29.
DR Pfam; PF07645; EGF_CA; 3.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF06816; NOD; 1.
DR Pfam; PF07684; NODP; 1.
DR Pfam; PF00066; Notch; 3.
DR PIRSF; PIRSF002279; Notch; 1.
DR PRINTS; PR01452; LNOTCHREPEAT.
DR PRINTS; PR01984; NOTCH1.
DR SMART; SM00248; ANK; 6.
DR SMART; SM01334; DUF3454; 1.
DR SMART; SM00181; EGF; 36.
DR SMART; SM00179; EGF_CA; 33.
DR SMART; SM00004; NL; 3.
DR SMART; SM01338; NOD; 1.
DR SMART; SM01339; NODP; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF57184; SSF57184; 6.
DR SUPFAM; SSF90193; SSF90193; 3.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 23.
DR PROSITE; PS00022; EGF_1; 34.
DR PROSITE; PS01186; EGF_2; 29.
DR PROSITE; PS50026; EGF_3; 36.
DR PROSITE; PS01187; EGF_CA; 22.
DR PROSITE; PS50258; LNR; 3.
PE 1: Evidence at protein level;
KW Activator; Angiogenesis; ANK repeat; Calcium; Cell membrane;
KW Developmental protein; Differentiation; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Metal-binding; Notch signaling pathway; Nucleus;
KW Receptor; Reference proteome; Repeat; Signal; Transcription;
KW Transcription regulation; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..2522
FT /note="Neurogenic locus notch homolog protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000425209"
FT CHAIN 1715..2522
FT /note="Notch 1 extracellular truncation"
FT /evidence="ECO:0000250"
FT /id="PRO_0000425210"
FT CHAIN 1749..2522
FT /note="Notch 1 intracellular domain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000425211"
FT TOPO_DOM 20..1730
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1731..1751
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P46531"
FT TOPO_DOM 1752..2522
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 20..57
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 58..99
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 102..140
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 141..177
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 179..215
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 217..254
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 256..292
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 294..332
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 334..370
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 371..409
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 411..449
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 451..487
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 489..525
FT /note="EGF-like 13; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 527..563
FT /note="EGF-like 14; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 565..600
FT /note="EGF-like 15; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 602..638
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 640..675
FT /note="EGF-like 17; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 677..713
FT /note="EGF-like 18; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 715..750
FT /note="EGF-like 19; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 752..788
FT /note="EGF-like 20; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 790..826
FT /note="EGF-like 21; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 828..866
FT /note="EGF-like 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 868..904
FT /note="EGF-like 23; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 906..942
FT /note="EGF-like 24; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 944..980
FT /note="EGF-like 25; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 982..1018
FT /note="EGF-like 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1020..1056
FT /note="EGF-like 27; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1058..1094
FT /note="EGF-like 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1096..1142
FT /note="EGF-like 29"
FT /evidence="ECO:0000305"
FT DOMAIN 1144..1180
FT /note="EGF-like 30; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1182..1218
FT /note="EGF-like 31; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1220..1264
FT /note="EGF-like 32; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1266..1304
FT /note="EGF-like 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1306..1345
FT /note="EGF-like 34"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1347..1383
FT /note="EGF-like 35"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1386..1424
FT /note="EGF-like 36"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1447..1487
FT /note="LNR 1"
FT REPEAT 1488..1529
FT /note="LNR 2"
FT REPEAT 1530..1564
FT /note="LNR 3"
FT REPEAT 1877..1920
FT /note="ANK 1"
FT REPEAT 1925..1954
FT /note="ANK 2"
FT REPEAT 1958..1988
FT /note="ANK 3"
FT REPEAT 1992..2021
FT /note="ANK 4"
FT REPEAT 2025..2054
FT /note="ANK 5"
FT REPEAT 2058..2087
FT /note="ANK 6"
FT REGION 2146..2229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2365..2404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2449..2522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2160..2182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2183..2197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2214..2229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2449..2473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2481..2515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 431
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT BINDING 434
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT BINDING 451
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT BINDING 452
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT BINDING 454
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT BINDING 489
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT BINDING 490
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT BINDING 492
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT BINDING 506
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT BINDING 507
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT BINDING 1458
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT BINDING 1473
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT BINDING 1476
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT BINDING 1500
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT BINDING 1515
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT BINDING 1518
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT BINDING 1540
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT BINDING 1555
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT BINDING 1558
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT SITE 1658..1659
FT /note="Cleavage; by furin-like protease"
FT /evidence="ECO:0000250|UniProtKB:Q01705"
FT SITE 1714..1715
FT /note="Cleavage; by adam17"
FT /evidence="ECO:0000250|UniProtKB:Q01705"
FT CARBOHYD 231
FT /note="O-linked (Fuc...) threonine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q01705"
FT CARBOHYD 231
FT /note="O-linked (GalNAc...) threonine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q01705"
FT CARBOHYD 434
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT CARBOHYD 457
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT CARBOHYD 465
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT CARBOHYD 495
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT CARBOHYD 887
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 958
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1400
FT /note="O-linked (Fuc...) threonine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q01705"
FT CARBOHYD 1400
FT /note="O-linked (GalNAc...) threonine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q01705"
FT CARBOHYD 1487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 22..35
FT /evidence="ECO:0000250"
FT DISULFID 29..45
FT /evidence="ECO:0000250"
FT DISULFID 47..56
FT /evidence="ECO:0000250"
FT DISULFID 62..74
FT /evidence="ECO:0000250"
FT DISULFID 68..87
FT /evidence="ECO:0000250"
FT DISULFID 89..98
FT /evidence="ECO:0000250"
FT DISULFID 106..117
FT /evidence="ECO:0000250"
FT DISULFID 111..128
FT /evidence="ECO:0000250"
FT DISULFID 130..139
FT /evidence="ECO:0000250"
FT DISULFID 145..156
FT /evidence="ECO:0000250"
FT DISULFID 150..165
FT /evidence="ECO:0000250"
FT DISULFID 167..176
FT /evidence="ECO:0000250"
FT DISULFID 183..194
FT /evidence="ECO:0000250"
FT DISULFID 188..203
FT /evidence="ECO:0000250"
FT DISULFID 205..214
FT /evidence="ECO:0000250"
FT DISULFID 221..232
FT /evidence="ECO:0000250"
FT DISULFID 226..242
FT /evidence="ECO:0000250"
FT DISULFID 244..253
FT /evidence="ECO:0000250"
FT DISULFID 260..271
FT /evidence="ECO:0000250"
FT DISULFID 265..280
FT /evidence="ECO:0000250"
FT DISULFID 282..291
FT /evidence="ECO:0000250"
FT DISULFID 298..311
FT /evidence="ECO:0000250"
FT DISULFID 305..320
FT /evidence="ECO:0000250"
FT DISULFID 322..331
FT /evidence="ECO:0000250"
FT DISULFID 338..349
FT /evidence="ECO:0000250"
FT DISULFID 343..358
FT /evidence="ECO:0000250"
FT DISULFID 360..369
FT /evidence="ECO:0000250"
FT DISULFID 375..386
FT /evidence="ECO:0000250"
FT DISULFID 380..397
FT /evidence="ECO:0000250"
FT DISULFID 399..408
FT /evidence="ECO:0000250"
FT DISULFID 415..428
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT DISULFID 422..437
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT DISULFID 439..448
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT DISULFID 455..466
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT DISULFID 460..475
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT DISULFID 477..486
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT DISULFID 493..504
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT DISULFID 498..513
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT DISULFID 515..524
FT /evidence="ECO:0000250|UniProtKB:Q07008"
FT DISULFID 531..542
FT /evidence="ECO:0000250"
FT DISULFID 536..551
FT /evidence="ECO:0000250"
FT DISULFID 553..562
FT /evidence="ECO:0000250"
FT DISULFID 569..579
FT /evidence="ECO:0000250"
FT DISULFID 574..588
FT /evidence="ECO:0000250"
FT DISULFID 590..599
FT /evidence="ECO:0000250"
FT DISULFID 606..617
FT /evidence="ECO:0000250"
FT DISULFID 611..626
FT /evidence="ECO:0000250"
FT DISULFID 628..637
FT /evidence="ECO:0000250"
FT DISULFID 644..654
FT /evidence="ECO:0000250"
FT DISULFID 649..663
FT /evidence="ECO:0000250"
FT DISULFID 665..674
FT /evidence="ECO:0000250"
FT DISULFID 681..692
FT /evidence="ECO:0000250"
FT DISULFID 686..701
FT /evidence="ECO:0000250"
FT DISULFID 703..712
FT /evidence="ECO:0000250"
FT DISULFID 719..729
FT /evidence="ECO:0000250"
FT DISULFID 724..738
FT /evidence="ECO:0000250"
FT DISULFID 740..749
FT /evidence="ECO:0000250"
FT DISULFID 756..767
FT /evidence="ECO:0000250"
FT DISULFID 761..776
FT /evidence="ECO:0000250"
FT DISULFID 778..787
FT /evidence="ECO:0000250"
FT DISULFID 794..805
FT /evidence="ECO:0000250"
FT DISULFID 799..814
FT /evidence="ECO:0000250"
FT DISULFID 816..825
FT /evidence="ECO:0000250"
FT DISULFID 832..843
FT /evidence="ECO:0000250"
FT DISULFID 837..854
FT /evidence="ECO:0000250"
FT DISULFID 856..865
FT /evidence="ECO:0000250"
FT DISULFID 872..883
FT /evidence="ECO:0000250"
FT DISULFID 877..892
FT /evidence="ECO:0000250"
FT DISULFID 894..903
FT /evidence="ECO:0000250"
FT DISULFID 910..921
FT /evidence="ECO:0000250"
FT DISULFID 915..930
FT /evidence="ECO:0000250"
FT DISULFID 932..941
FT /evidence="ECO:0000250"
FT DISULFID 948..959
FT /evidence="ECO:0000250"
FT DISULFID 953..968
FT /evidence="ECO:0000250"
FT DISULFID 970..979
FT /evidence="ECO:0000250"
FT DISULFID 986..997
FT /evidence="ECO:0000250"
FT DISULFID 991..1006
FT /evidence="ECO:0000250"
FT DISULFID 1008..1017
FT /evidence="ECO:0000250"
FT DISULFID 1024..1035
FT /evidence="ECO:0000250"
FT DISULFID 1029..1044
FT /evidence="ECO:0000250"
FT DISULFID 1046..1055
FT /evidence="ECO:0000250"
FT DISULFID 1062..1073
FT /evidence="ECO:0000250"
FT DISULFID 1067..1082
FT /evidence="ECO:0000250"
FT DISULFID 1084..1093
FT /evidence="ECO:0000250"
FT DISULFID 1100..1121
FT /evidence="ECO:0000305"
FT DISULFID 1115..1130
FT /evidence="ECO:0000250"
FT DISULFID 1132..1141
FT /evidence="ECO:0000250"
FT DISULFID 1148..1159
FT /evidence="ECO:0000250"
FT DISULFID 1153..1168
FT /evidence="ECO:0000250"
FT DISULFID 1170..1179
FT /evidence="ECO:0000250"
FT DISULFID 1186..1197
FT /evidence="ECO:0000250"
FT DISULFID 1191..1206
FT /evidence="ECO:0000250"
FT DISULFID 1208..1217
FT /evidence="ECO:0000250"
FT DISULFID 1224..1243
FT /evidence="ECO:0000250"
FT DISULFID 1237..1252
FT /evidence="ECO:0000250"
FT DISULFID 1254..1263
FT /evidence="ECO:0000250"
FT DISULFID 1270..1283
FT /evidence="ECO:0000250"
FT DISULFID 1275..1292
FT /evidence="ECO:0000250"
FT DISULFID 1294..1303
FT /evidence="ECO:0000250"
FT DISULFID 1310..1321
FT /evidence="ECO:0000250"
FT DISULFID 1315..1333
FT /evidence="ECO:0000250"
FT DISULFID 1335..1344
FT /evidence="ECO:0000250"
FT DISULFID 1351..1362
FT /evidence="ECO:0000250"
FT DISULFID 1356..1371
FT /evidence="ECO:0000250"
FT DISULFID 1373..1382
FT /evidence="ECO:0000250"
FT DISULFID 1390..1401
FT /evidence="ECO:0000250"
FT DISULFID 1395..1412
FT /evidence="ECO:0000250"
FT DISULFID 1414..1423
FT /evidence="ECO:0000250"
FT DISULFID 1447..1470
FT /evidence="ECO:0000250"
FT DISULFID 1452..1465
FT /evidence="ECO:0000250"
FT DISULFID 1461..1477
FT /evidence="ECO:0000250"
FT DISULFID 1488..1512
FT /evidence="ECO:0000250"
FT DISULFID 1494..1507
FT /evidence="ECO:0000250"
FT DISULFID 1503..1519
FT /evidence="ECO:0000250"
FT DISULFID 1534..1547
FT /evidence="ECO:0000250"
FT DISULFID 1543..1559
FT /evidence="ECO:0000250"
FT CONFLICT 527
FT /note="D -> H (in Ref. 2; AAI33054)"
FT /evidence="ECO:0000305"
FT CONFLICT 1015
FT /note="N -> D (in Ref. 2; AAI33054)"
FT /evidence="ECO:0000305"
FT CONFLICT 1244
FT /note="F -> I (in Ref. 2; AAI33054)"
FT /evidence="ECO:0000305"
FT CONFLICT 2239
FT /note="L -> P (in Ref. 2; AAI33054)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2522 AA; 274530 MW; 1425E154A4BC5BCD CRC64;
MYRIGLLVLI WSLLGLAQGL RCTQTAEMCL NGGRCEMTPG GTGVCLCSSS YFGERCQYPN
PCALKNQCMN FGTCEPVLLG NAIDFTCHCP VGFTDKVCLT PVDNACVNNP CRNGGTCELL
SSVSDYRCRC PPGWTGDSCQ QADPCASNPC ANGGKCLPFE TQYICKCPSG FHGATCKQDI
NECSQNPCRN GGQCLNEFGS YRCNCQNRFT GRNCEEPYVP CNPSPCLNGG TCRQTDDTSY
ECTCLPGFSG QNCEENIDDC PSNNCRNGGT CVDGVNTYNC QCPPDWTGQY CTEDVDECQL
MPNACQNGGT CHNTYGGYNC VCVNGWTGED CSENIDDCAN AACHSGATCH DRVASFFCEC
PHGRTGLLCH LDNACISNPC NEGSNCDTNP VNGKAICTCP PGYTGPACNN DVDECSLGAN
PCEHGGRCTN TLGSFQCNCP QGYAGPRCEI DVNECLSNPC QNDATCLDQI GEFQCICMPG
YEGLYCETNI DECASNPCLH NGKCVDKINE FHCECPTGFN GNLCQHDVDE CASTPCKNGA
KCLDGPNSYT CQCTEGFTGR HCEQDINECI PDPCHYGTCK DGIATFTCLC RPGYTGRLCD
NDINECLSQP CQNGGQCTDR ENGYICTCPK GTTGVNCETN LDDCASNPCD YGKCIDKIDG
YECTCEPGYT GKMCNINIDE CASNPCRNGG TCKDKINGFT CVCPDGYHDH MCLSEVNECN
SNPCIHGTCH DGINGYKCDC DAGWSGSNCD VNNNECESNP CMNGGTCKDM TGAYICTCRA
GFSGPNCQTN INECASNPCL NRGTCIDDVA GYKCNCMLPY TGAICEAVLA PCSGSPCKNG
GRCKESEDYE TFSCECPPGW QGQTCEIDMN ECVNRPCRNG AMCQNTNGSY KCNCKPGYAG
RHCETDIDDC QPNPCHNGGS CSDGINMFFC NCPAGFRGPK CEEDINECAS NPCKNGANCT
DCVNSYTCTC QPGFSGIHCE NNTPDCTESS CFNGGTCIDG INTFSCQCPP GFTGNYCQHD
INECDSKPCL NGGTCQDSYG AYKCTCPQGY TGLNCQNLVR WCDSSPCKNG GKCWQTNNFY
RCECKSGWTG VYCDVPSVSC EVAAKQQGVD IAHLCRNSGM CVDTGNTHFC RCQAGYTGSY
CEEQVDECSP NPCQNGATCT DYLGGYSCEC VAGYHGVNCS EEINECLSHP CHNGGTCIDL
INTYKCSCPR GTQGVHCEIN VDDCTPFYDS VSLEPKCFNN GKCFDRVGGY NCICPPGFVG
ERCEGDVNEC LSNPCDPRGT QNCIQLVNDY RCECRQGFTG RRCDSVVDGC KGLPCRNGGT
CAVASNTERG FICKCPPGFD GATCEYDART CGNLRCQNGG TCISVLKSSK CVCSEGYTGA
TCQYPVVSPC ASRPCYNGGT CQFSPEEPFF QCFCPTNFNG LFCHILDYGF IGGLGKNITP
PDNEEICENE QCAELADNKI CNANCNNHAC GWDGGDCSLN FNDPWKNCTQ SLQCWKYFND
GKCDSQCNNS GCLYDGFDCQ KVEVQCNPLY DQYCRDHFQD GHCDQGCNNA ECEWDGLDCD
NMPENLAEGT LLIVVLMPPE KLKNNSVNFL RELSRVLHTN VVFKKDSKGE YKIYPYYGNE
EELKKHHIKK RSAASWSDAP TAIFSTMKES VLPGRRRREL DQMEVRGSIV YLEIDNRQCY
KSSSQCFTSA TDVAAFLGAL ATHGNLNIPY KIEAVKSEIV ETAKPPPPLY AMFSMLVIPL
LIIFVIMVVI VNKKRRREHG QLWFPEGFIP KEPSKKKRRE PLGEDSVGLK PLKNLTDGSF
MDDNQNEWGD EETLENKRFR FEEQVMLPEL VDDQTDHRQW TQQHLDAADL RIPSMAPTPP
QGEIDADCMD VNVRGPDGFT PLMIAACSGG GLETGNSEEE EDASANMISD FIGQGAQLHN
QTDRTGETAL HLAARYARAD AAKRLLESSA DANVPDNMGR TPLHAAVAAD AQGVFQILIR
NRATDLDARM CDGTTPLILA ARLAVEGMVE ELINAHADVN AVDEFGKSAL HWAAAVNNVD
AAAVLLKSSA NKDMQNNKEE TPLFLAAREG SYETAKVLLD HYANRDITDH MDRLPRDIAQ
ERMHHDIVHL LDEHNLVKSP TLHGGPLGAP TLSPPICSPN GYMGNMKPSV QSKKARKPSI
KGNGCKEAKE LKARRKKSQD GKTSLLDSGS SGVLSPVDSL ESPHGYLSDV ASPPLMTSPF
QQSPSMPLNH LTSMQDSHLG LNHMTMANKQ EMASNRMAFD GMTPRLTHLN VSSPNTIMTN
GSMHFTVGGA PAMNGQCDWF ARLQNGMVQN QYNPIRNGIQ QGNAQQALQH GLMSSLHNGL
PATTLSQMMT YQAMPNTRMA NQPHLMQAQQ MQQQQNLQLH QSVQQQQHQN SNATSTHIGS
PFCSNDISQT DLQQMSGNNI HSVMPQDTQI FTNSLPPTLT QSMATTQFLT PPSQHSYSSP
MDNTPSHQLQ VPDHPFLTPS PESPDQWSSS SPHSNMSDWS EGISSPPTSM QPQRTHIPEA
FK
