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DLL3_RAT
ID   DLL3_RAT                Reviewed;         589 AA.
AC   O88671;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Delta-like protein 3;
DE   AltName: Full=Drosophila Delta homolog 3;
DE            Short=Delta3;
DE   Flags: Precursor;
GN   Name=Dll3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Boulter J., Greenfield A., Weinmaster G.;
RT   "Rattus norvegicus mRNA for Delta 3: a putative ligand for Notch.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Inhibits primary neurogenesis. May be required to divert
CC       neurons along a specific differentiation pathway. Plays a role in the
CC       formation of somite boundaries during segmentation of the paraxial
CC       mesoderm (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Can bind and activate Notch-1 or another Notch receptor.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The DSL domain is required for binding to the Notch receptor.
CC   -!- PTM: Ubiquitinated by MIB (MIB1 or MIB2), leading to its endocytosis
CC       and subsequent degradation. {ECO:0000250}.
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DR   EMBL; AF084576; AAC33303.1; -; mRNA.
DR   RefSeq; NP_446118.1; NM_053666.1.
DR   AlphaFoldDB; O88671; -.
DR   SMR; O88671; -.
DR   STRING; 10116.ENSRNOP00000026182; -.
DR   PaxDb; O88671; -.
DR   PRIDE; O88671; -.
DR   ABCD; O88671; 8 sequenced antibodies.
DR   GeneID; 114125; -.
DR   KEGG; rno:114125; -.
DR   UCSC; RGD:70953; rat.
DR   CTD; 10683; -.
DR   RGD; 70953; Dll3.
DR   eggNOG; KOG1217; Eukaryota.
DR   InParanoid; O88671; -.
DR   OrthoDB; 394787at2759; -.
DR   PhylomeDB; O88671; -.
DR   PRO; PR:O88671; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005112; F:Notch binding; IPI:RGD.
DR   GO; GO:0001709; P:cell fate determination; TAS:RGD.
DR   GO; GO:0007417; P:central nervous system development; IEP:RGD.
DR   GO; GO:0007386; P:compartment pattern specification; ISO:RGD.
DR   GO; GO:0048712; P:negative regulation of astrocyte differentiation; IDA:RGD.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; ISO:RGD.
DR   GO; GO:0045746; P:negative regulation of Notch signaling pathway; IDA:RGD.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0048339; P:paraxial mesoderm development; ISO:RGD.
DR   GO; GO:0050769; P:positive regulation of neurogenesis; IDA:RGD.
DR   GO; GO:0001501; P:skeletal system development; ISS:UniProtKB.
DR   GO; GO:0001756; P:somitogenesis; ISO:RGD.
DR   GO; GO:0009888; P:tissue development; ISO:RGD.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF12661; hEGF; 3.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00179; EGF_CA; 5.
DR   PROSITE; PS00022; EGF_1; 6.
DR   PROSITE; PS01186; EGF_2; 5.
DR   PROSITE; PS50026; EGF_3; 6.
PE   2: Evidence at transcript level;
KW   Developmental protein; Differentiation; Disulfide bond; EGF-like domain;
KW   Membrane; Notch signaling pathway; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix; Ubl conjugation.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000250"
FT   CHAIN           33..589
FT                   /note="Delta-like protein 3"
FT                   /id="PRO_0000007511"
FT   TOPO_DOM        33..494
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        495..515
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        516..589
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          174..213
FT                   /note="DSL"
FT   DOMAIN          218..251
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          276..312
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          314..353
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          355..391
FT                   /note="EGF-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          393..429
FT                   /note="EGF-like 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          431..467
FT                   /note="EGF-like 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REGION          552..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        222..233
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        226..239
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        241..250
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        280..291
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        285..300
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        302..311
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        318..329
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        323..341
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        343..352
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        359..370
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        364..379
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        381..390
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        397..408
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        402..417
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        419..428
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        435..446
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        440..455
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        457..466
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   589 AA;  61425 MW;  A17B3BF9B95EC17F CRC64;
     MVSLQVSSLP QTLILAFLLP QALPAGVFEL QIHSFGPGPG PGTPRSPCNA RGPCRLFFRV
     CLKPGVSQEA AESLCALGAA LSTSGPVYTE QPGVPAAALS LPDGLVRVPF LDAWPGTFSL
     IIETWREQLG ERAAGPAWNL LARVAGRRRL AAGAPWARDV QRTGAWELHF SYRARCEPPA
     VGAACARLCR SRSAPSRCGP GLRPCTPFPD ECEAPRESLT VCRAGCSPEH GYCEEPDECH
     CLEGWTGPLC TVPVSTSSCL NSRVSGPAGT GCLLPGPGPC DGNPCANGGS CSETPGSFEC
     ACPRGFYGPR CEVSGVTCAD GPCFNGGLCV GGEDPDSAYV CHCPPAFQGS NCERRVDRCS
     LQPCQNGGLC LDLGHALRCR CRAGFAGPRC EHDLDDCAGR ACANGGTCVE GGGARRCSCA
     LGFGGRDCRE RADPCASRPC AHGGRCYAHF SGLVCACAPG YMGVRCEFAV RPDGADAVPA
     APRGLRQADS QRFLLPPALG LLAAAALAGA ALLLIHVRRR GPGRDTGTRL LSGTREPSVH
     TLPDALNNLR LQDGAGDGPT SSADWNHPED GDSRSIYVIP APSIYAREA
 
 
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