NOTC1_DANRE
ID NOTC1_DANRE Reviewed; 2437 AA.
AC P46530;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 175.
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=notch1a; Synonyms=notch;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=8297791; DOI=10.1016/0925-4773(93)90027-u;
RA Bierkamp C., Campos-Ortega J.A.;
RT "A zebrafish homologue of the Drosophila neurogenic gene Notch and its
RT pattern of transcription during early embryogenesis.";
RL Mech. Dev. 43:87-100(1993).
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) (By similarity).
CC {ECO:0000250|UniProtKB:Q01705}.
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 -!- DEVELOPMENTAL STAGE: Expressed in all cells in pregastrulation stages.
CC During gastrulation is differentially expressed, accumulating
CC predominantly in the prechordal mesoderm and notochord. At the end of
CC gastrulation, expressed along the anterior-posterior axis including the
CC developing neural plate and differentiating mesoderm. Also present in
CC the developing brain and head regions.
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 -!- 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) (By similarity).
CC {ECO:0000250|UniProtKB:Q01705}.
CC -!- SIMILARITY: Belongs to the NOTCH family. {ECO:0000305}.
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DR EMBL; X69088; CAA48831.1; -; mRNA.
DR PIR; S42612; S42612.
DR RefSeq; NP_571516.1; NM_131441.1.
DR AlphaFoldDB; P46530; -.
DR SMR; P46530; -.
DR BioGRID; 78873; 3.
DR STRING; 7955.ENSDARP00000046632; -.
DR PaxDb; P46530; -.
DR GeneID; 30718; -.
DR KEGG; dre:30718; -.
DR CTD; 30718; -.
DR ZFIN; ZDB-GENE-990415-173; notch1a.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; P46530; -.
DR OrthoDB; 7525at2759; -.
DR PhylomeDB; P46530; -.
DR SignaLink; P46530; -.
DR PRO; PR:P46530; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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:0009952; P:anterior/posterior pattern specification; IMP:ZFIN.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:ZFIN.
DR GO; GO:0035907; P:dorsal aorta development; IMP:ZFIN.
DR GO; GO:0031017; P:exocrine pancreas development; IMP:ZFIN.
DR GO; GO:0048699; P:generation of neurons; IMP:ZFIN.
DR GO; GO:0021986; P:habenula development; IMP:ZFIN.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:ZFIN.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IMP:ZFIN.
DR GO; GO:0055016; P:hypochord development; IMP:ZFIN.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IGI:ZFIN.
DR GO; GO:0001840; P:neural plate development; IGI:ZFIN.
DR GO; GO:0061314; P:Notch signaling involved in heart development; ISS:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IMP:ZFIN.
DR GO; GO:0031016; P:pancreas development; IMP:ZFIN.
DR GO; GO:0048936; P:peripheral nervous system neuron axonogenesis; IGI:ZFIN.
DR GO; GO:0048337; P:positive regulation of mesodermal cell fate specification; IMP:ZFIN.
DR GO; GO:0042663; P:regulation of endodermal cell fate specification; IMP:ZFIN.
DR GO; GO:0048259; P:regulation of receptor-mediated endocytosis; IGI:ZFIN.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0021523; P:somatic motor neuron differentiation; IMP:ZFIN.
DR GO; GO:0001756; P:somitogenesis; IMP:ZFIN.
DR GO; GO:0021531; P:spinal cord radial glial cell differentiation; IMP:ZFIN.
DR GO; GO:0021514; P:ventral spinal cord interneuron differentiation; IMP:ZFIN.
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; 23.
DR Pfam; PF07645; EGF_CA; 4.
DR Pfam; PF12661; hEGF; 4.
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; 32.
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; 28.
DR PROSITE; PS50026; EGF_3; 36.
DR PROSITE; PS01187; EGF_CA; 22.
DR PROSITE; PS50258; LNR; 3.
PE 2: Evidence at transcript 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..2437
FT /note="Neurogenic locus notch homolog protein 1"
FT /id="PRO_0000007708"
FT CHAIN 1713..2437
FT /note="Notch 1 extracellular truncation"
FT /evidence="ECO:0000250"
FT /id="PRO_0000425200"
FT CHAIN 1745..2437
FT /note="Notch 1 intracellular domain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000425201"
FT TOPO_DOM 21..1726
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1727..1747
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P46531"
FT TOPO_DOM 1748..2437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 21..57
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 58..98
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 101..138
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 139..175
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 177..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..524
FT /note="EGF-like 13; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 526..562
FT /note="EGF-like 14; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 564..599
FT /note="EGF-like 15; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 601..637
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 639..674
FT /note="EGF-like 17; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 676..712
FT /note="EGF-like 18; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 714..749
FT /note="EGF-like 19; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 751..787
FT /note="EGF-like 20; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 789..825
FT /note="EGF-like 21; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 827..865
FT /note="EGF-like 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 867..903
FT /note="EGF-like 23; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 905..941
FT /note="EGF-like 24; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 943..979
FT /note="EGF-like 25; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 981..1017
FT /note="EGF-like 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1019..1055
FT /note="EGF-like 27; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1057..1093
FT /note="EGF-like 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1095..1141
FT /note="EGF-like 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1143..1179
FT /note="EGF-like 30; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1181..1217
FT /note="EGF-like 31; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1219..1263
FT /note="EGF-like 32; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1265..1303
FT /note="EGF-like 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1305..1344
FT /note="EGF-like 34"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1346..1382
FT /note="EGF-like 35"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1385..1423
FT /note="EGF-like 36"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1447..1487
FT /note="LNR 1"
FT REPEAT 1488..1525
FT /note="LNR 2"
FT REPEAT 1526..1566
FT /note="LNR 3"
FT REPEAT 1867..1910
FT /note="ANK 1"
FT REPEAT 1915..1944
FT /note="ANK 2"
FT REPEAT 1948..1978
FT /note="ANK 3"
FT REPEAT 1982..2011
FT /note="ANK 4"
FT REPEAT 2015..2044
FT /note="ANK 5"
FT REPEAT 2048..2077
FT /note="ANK 6"
FT REGION 1770..1790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2127..2174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2356..2437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2127..2141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2146..2169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2356..2429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 1656..1657
FT /note="Cleavage; by furin-like protease"
FT /evidence="ECO:0000250|UniProtKB:Q01705"
FT SITE 1712..1713
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 957
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1399
FT /note="O-linked (Fuc...) threonine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q01705"
FT CARBOHYD 1399
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 1585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 25..35
FT /evidence="ECO:0000250"
FT DISULFID 29..45
FT /evidence="ECO:0000250"
FT DISULFID 47..56
FT /evidence="ECO:0000250"
FT DISULFID 62..73
FT /evidence="ECO:0000250"
FT DISULFID 67..86
FT /evidence="ECO:0000250"
FT DISULFID 88..97
FT /evidence="ECO:0000250"
FT DISULFID 105..116
FT /evidence="ECO:0000250"
FT DISULFID 110..126
FT /evidence="ECO:0000250"
FT DISULFID 128..137
FT /evidence="ECO:0000250"
FT DISULFID 143..154
FT /evidence="ECO:0000250"
FT DISULFID 148..163
FT /evidence="ECO:0000250"
FT DISULFID 165..174
FT /evidence="ECO:0000250"
FT DISULFID 181..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"
FT DISULFID 422..437
FT /evidence="ECO:0000250"
FT DISULFID 439..448
FT /evidence="ECO:0000250"
FT DISULFID 455..466
FT /evidence="ECO:0000250"
FT DISULFID 460..475
FT /evidence="ECO:0000250"
FT DISULFID 477..486
FT /evidence="ECO:0000250"
FT DISULFID 493..503
FT /evidence="ECO:0000250"
FT DISULFID 498..512
FT /evidence="ECO:0000250"
FT DISULFID 514..523
FT /evidence="ECO:0000250"
FT DISULFID 530..541
FT /evidence="ECO:0000250"
FT DISULFID 535..550
FT /evidence="ECO:0000250"
FT DISULFID 552..561
FT /evidence="ECO:0000250"
FT DISULFID 568..578
FT /evidence="ECO:0000250"
FT DISULFID 573..587
FT /evidence="ECO:0000250"
FT DISULFID 589..598
FT /evidence="ECO:0000250"
FT DISULFID 605..616
FT /evidence="ECO:0000250"
FT DISULFID 610..625
FT /evidence="ECO:0000250"
FT DISULFID 627..636
FT /evidence="ECO:0000250"
FT DISULFID 643..653
FT /evidence="ECO:0000250"
FT DISULFID 648..662
FT /evidence="ECO:0000250"
FT DISULFID 664..673
FT /evidence="ECO:0000250"
FT DISULFID 680..691
FT /evidence="ECO:0000250"
FT DISULFID 685..700
FT /evidence="ECO:0000250"
FT DISULFID 702..711
FT /evidence="ECO:0000250"
FT DISULFID 718..728
FT /evidence="ECO:0000250"
FT DISULFID 723..737
FT /evidence="ECO:0000250"
FT DISULFID 739..748
FT /evidence="ECO:0000250"
FT DISULFID 755..766
FT /evidence="ECO:0000250"
FT DISULFID 760..775
FT /evidence="ECO:0000250"
FT DISULFID 777..786
FT /evidence="ECO:0000250"
FT DISULFID 793..804
FT /evidence="ECO:0000250"
FT DISULFID 798..813
FT /evidence="ECO:0000250"
FT DISULFID 815..824
FT /evidence="ECO:0000250"
FT DISULFID 831..842
FT /evidence="ECO:0000250"
FT DISULFID 836..853
FT /evidence="ECO:0000250"
FT DISULFID 855..864
FT /evidence="ECO:0000250"
FT DISULFID 871..882
FT /evidence="ECO:0000250"
FT DISULFID 876..891
FT /evidence="ECO:0000250"
FT DISULFID 893..902
FT /evidence="ECO:0000250"
FT DISULFID 909..920
FT /evidence="ECO:0000250"
FT DISULFID 914..929
FT /evidence="ECO:0000250"
FT DISULFID 931..940
FT /evidence="ECO:0000250"
FT DISULFID 947..958
FT /evidence="ECO:0000250"
FT DISULFID 952..967
FT /evidence="ECO:0000250"
FT DISULFID 969..978
FT /evidence="ECO:0000250"
FT DISULFID 985..996
FT /evidence="ECO:0000250"
FT DISULFID 990..1005
FT /evidence="ECO:0000250"
FT DISULFID 1007..1016
FT /evidence="ECO:0000250"
FT DISULFID 1023..1034
FT /evidence="ECO:0000250"
FT DISULFID 1028..1043
FT /evidence="ECO:0000250"
FT DISULFID 1045..1054
FT /evidence="ECO:0000250"
FT DISULFID 1061..1072
FT /evidence="ECO:0000250"
FT DISULFID 1066..1081
FT /evidence="ECO:0000250"
FT DISULFID 1083..1092
FT /evidence="ECO:0000250"
FT DISULFID 1099..1120
FT /evidence="ECO:0000250|UniProtKB:P46531"
FT DISULFID 1114..1129
FT /evidence="ECO:0000250"
FT DISULFID 1131..1140
FT /evidence="ECO:0000250"
FT DISULFID 1147..1158
FT /evidence="ECO:0000250"
FT DISULFID 1152..1167
FT /evidence="ECO:0000250"
FT DISULFID 1169..1178
FT /evidence="ECO:0000250"
FT DISULFID 1185..1196
FT /evidence="ECO:0000250"
FT DISULFID 1190..1205
FT /evidence="ECO:0000250"
FT DISULFID 1207..1216
FT /evidence="ECO:0000250"
FT DISULFID 1223..1242
FT /evidence="ECO:0000250"
FT DISULFID 1236..1251
FT /evidence="ECO:0000250"
FT DISULFID 1253..1262
FT /evidence="ECO:0000250"
FT DISULFID 1269..1282
FT /evidence="ECO:0000250"
FT DISULFID 1274..1291
FT /evidence="ECO:0000250"
FT DISULFID 1293..1302
FT /evidence="ECO:0000250"
FT DISULFID 1309..1320
FT /evidence="ECO:0000250"
FT DISULFID 1314..1332
FT /evidence="ECO:0000250"
FT DISULFID 1334..1343
FT /evidence="ECO:0000250"
FT DISULFID 1350..1361
FT /evidence="ECO:0000250"
FT DISULFID 1355..1370
FT /evidence="ECO:0000250"
FT DISULFID 1372..1381
FT /evidence="ECO:0000250"
FT DISULFID 1389..1400
FT /evidence="ECO:0000250"
FT DISULFID 1394..1411
FT /evidence="ECO:0000250"
FT DISULFID 1413..1422
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 1526..1552
FT /evidence="ECO:0000250"
FT DISULFID 1534..1547
FT /evidence="ECO:0000250"
FT DISULFID 1543..1559
FT /evidence="ECO:0000250"
SQ SEQUENCE 2437 AA; 262308 MW; D8C21012AA4CA8FC CRC64;
MNRFLVKLTL LTAASLATVA QGQRCSEYCQ NGGICEYKPS GEASCRCPAD FVGAQCQFPN
PCNPSPCRNG GVCRPQMQGN EVGVKCDCVL GFSDRLCLTP VNHACMNSPC RNGGTCSLLT
LDTFTCRCQP GWSGKTCQLA DPCASNPCAN GGQCSAFESH YICTCPPNFH GQTCRQDVNE
CAVSPSPCRN GGTCINEVGS YLCRCPPEYT GPHCQRLYQP CLPSPCRSGG TCVQTSDTTH
TCSCLPGFTG QTCEHNVDDC TQHACENGGP CIDGINTYNC HCDKHWTGQY CTEDVDECEL
SPNACQNGGT CHNTIGGFHC VCVNGWTGDD CSENIDDCAS AACSHGATCH DRVASFFCEC
PHGRTGLLCH LDDACISNPC QKGSNCDTNP VSGKAICTCP PGYTGSACNQ DIDECSLGAN
PCEHGGRCLN TKGSFQCKCL QGYEGPRCEM DVNECKSNPC QNDATCLDQI GGFHCICMPG
YEGVFCQINS DDCASQPCLN GKCIDKINSF HCECPKGFSG SLCQVDVDEC ASTPCKNGAK
CTDGPNKYTC ECTPGFSGIH CELDINECAS SPCHYGVCRD GVASFTCDCR PGYTGRLCET
NINECLSQPC RNGGTCQDRE NAYICTCPKG TTGVNCEINI DDCKRKPCDY GKCIDKINGY
ECVCEPGYSG SMCNINIDDC ALNPCHNGGT CIDGVNSFTC LCPDGFRDAT CLSQHNECSS
NPCIHGSCLD QINSYRCVCE AGWMGRNCDI NINECLSNPC VNGGTCKDMT SGYLCTCRAG
FSGPNCQMNI NECASNPCLN QGSCIDDVAG FKCNCMLPYT GEVCENVLAP CSPRPCKNGG
VCRESEDFQS FSCNCPAGWQ GQTCEVDINE CVRNPCTNGG VCENLRGGFQ CRCNPGFTGA
LCENDIDDCE PNPCSNGGVC QDRVNGFVCV CLAGFRGERC AEDIDECVSA PCRNGGNCTD
CVNSYTCSCP AGFSGINCEI NTPDCTESSC FNGGTCVDGI SSFSCVCLPG FTGNYCQHDV
NECDSRPCQN GGSCQDGYGT YKCTCPHGYT GLNCQSLVRW CDSSPCKNGG SCWQQGASFT
CQCASGWTGI YCDVPSVSCE VAARQQGVSV AVLCRHAGQC VDAGNTHLCR CQAGYTGSYC
QEQVDECQPN PCQNGATCTD YLGGYSCECV PGYHGMNCSK EINECLSQPC QNGGTCIDLV
NTYKCSCPRG TQGVHCEIDI DDCSPSVDPL TGEPRCFNGG RCVDRVGGYG CVCPAGFVGE
RCEGDVNECL SDPCDPSGSY NCVQLINDFR CECRTGYTGK RCETVFNGCK DTPCKNGGTC
AVASNTKHGY ICKCQPGYSG SSCEYDSQSC GSLRCRNGAT CVSGHLSPRC LCAPGFSGHE
CQTRMDSPCL VNPCYNGGTC QPISDAPFYR CSCPANFNGL LCHILDYSFS GGQGRDIAPP
VEVEIRCEIA QCEGRGGNAI CDTQCNNHAC GWDGGDCSLN FDDPWQNCSA ALQCWRYFND
GKCDEQCATA GCLYDGFDCQ RLEGQCNPLY DQYCRDHYAD GHCDQGCNNA ECEWDGLDCA
DDVPQKLAVG SLVLVVHIPP DELRNRSSSF LRELSSLLHT NVVFRRDANG EALIFPYYGS
EHELSKHKRS DWTDPGQLMQ RARRSLTSFL KPRTRRELDH MEVKGSIVYL EIDNRQCFQQ
SDECFQSATD VAAFLGALAS SGNLNVPYII EAVTSEGGPP KTGEMYPMFL VLLALAVLAL
AAVGVVVSRK RKREHGQLWF PEGFKVNEPK KKRREPVGED SVGLKPLKNS DSSLMDEQLS
EWAEDDTNKR FRFEGQSILE MSGQLDHRQW TQQHLDAADL RLNSMAPTPP QGQIENDCMD
VNVRGPDGFT PLMIASCSGG GLENENGEAE EDPSADVITD FIYHGANLHN QTDRTGETAL
HLAARYARSD AAKRLLESCA DANVQDNMGR TPLHAAVAAD AQGVFQILIR NRATDLDARM
HDGTTPLILA TRLAVEGMVE ELINCHADPN AVDDSGKSAL HWAAAVNNVD AAVVLLKNGA
NKDLQNNKEE TPLFLAAREG SYETAKVLLD HLANRDIADH LDQLPRDIAH ERMHHDIVRL
LEEYNLVRSP PLPLSPPLCC PNTYLGIKPS PGNNNNTAKK TRKPGGKGVG GKDSGKDIRT
KKKKSGDGKN GGIMEVGVLS PVDSLESPHG YLSDVSSPPM MTSPFQQSPP ISLNQLQGLA
DSHMGGALQG LGKPFDSAPR LSHLPVANNV GGAQAGACDW LQRVQQQQQQ QQQQQQAGML
MPTMLSATNM PQVMGYPTMQ SSHLGAPSHM IAHQNMAPMQ HQNISHHFLG DLSGLDLQSS
SGHAPIQTIL PQDSQRMAPP ISSTQFLTPP SQHSYSNPMD NTPNHQQVPD HPFLTPSAGS
PDQWSSSSPH SNLSDWSEGI SSPPTSMQMN HIPEAFK
