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EGF_FELCA
ID   EGF_FELCA               Reviewed;        1210 AA.
AC   Q95ND4;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Pro-epidermal growth factor;
DE            Short=EGF;
DE   Contains:
DE     RecName: Full=Epidermal growth factor;
DE   Flags: Precursor;
GN   Name=EGF;
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ohashi K., Takahashi N., Sugimoto C., Onuma M.;
RT   "Felis catus epidermal growth factor (EGF) cDNA.";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: EGF stimulates the growth of various epidermal and epithelial
CC       tissues in vivo and in vitro and of some fibroblasts in cell culture.
CC       Magnesiotropic hormone that stimulates magnesium reabsorption in the
CC       renal distal convoluted tubule via engagement of EGFR and activation of
CC       the magnesium channel TRPM6 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with EGFR and promotes EGFR dimerization. Interacts
CC       with RHBDF1; may retain EGF in the endoplasmic reticulum and regulates
CC       its degradation through the endoplasmic reticulum-associated
CC       degradation (ERAD) (By similarity). Interacts with RHBDF2 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
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DR   EMBL; AB050947; BAB47391.1; -; mRNA.
DR   RefSeq; NP_001009381.1; NM_001009381.1.
DR   AlphaFoldDB; Q95ND4; -.
DR   SMR; Q95ND4; -.
DR   STRING; 9685.ENSFCAP00000000470; -.
DR   PRIDE; Q95ND4; -.
DR   GeneID; 493978; -.
DR   KEGG; fca:493978; -.
DR   CTD; 1950; -.
DR   eggNOG; KOG1215; Eukaryota.
DR   InParanoid; Q95ND4; -.
DR   OrthoDB; 1174178at2759; -.
DR   Proteomes; UP000011712; 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:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0038029; P:epidermal growth factor receptor signaling pathway via MAPK cascade; ISS:UniProtKB.
DR   GO; GO:0043388; P:positive regulation of DNA binding; ISS:UniProtKB.
DR   GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
DR   GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; ISS:UniProtKB.
DR   Gene3D; 2.120.10.30; -; 2.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR026823; cEGF.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR016317; Pro-epidermal_GF.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF00058; Ldl_recept_b; 4.
DR   PIRSF; PIRSF001778; Pro-epidermal_growth_factor; 1.
DR   SMART; SM00181; EGF; 9.
DR   SMART; SM00179; EGF_CA; 6.
DR   SMART; SM00135; LY; 9.
DR   SUPFAM; SSF57184; SSF57184; 3.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 7.
DR   PROSITE; PS50026; EGF_3; 5.
DR   PROSITE; PS01187; EGF_CA; 3.
DR   PROSITE; PS51120; LDLRB; 9.
PE   2: Evidence at transcript level;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Growth factor; Membrane;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..1210
FT                   /note="Pro-epidermal growth factor"
FT                   /id="PRO_0000007538"
FT   CHAIN           969..1020
FT                   /note="Epidermal growth factor"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000007539"
FT   TOPO_DOM        23..1029
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1030..1050
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1051..1210
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          86..127
FT                   /note="LDL-receptor class B 1"
FT   REPEAT          128..169
FT                   /note="LDL-receptor class B 2"
FT   REPEAT          170..211
FT                   /note="LDL-receptor class B 3"
FT   REPEAT          212..258
FT                   /note="LDL-receptor class B 4"
FT   DOMAIN          312..352
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          353..393
FT                   /note="EGF-like 2; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          394..434
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          432..474
FT                   /note="EGF-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REPEAT          480..520
FT                   /note="LDL-receptor class B 5"
FT   REPEAT          521..563
FT                   /note="LDL-receptor class B 6"
FT   REPEAT          564..606
FT                   /note="LDL-receptor class B 7"
FT   REPEAT          607..650
FT                   /note="LDL-receptor class B 8"
FT   REPEAT          651..693
FT                   /note="LDL-receptor class B 9"
FT   DOMAIN          738..778
FT                   /note="EGF-like 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          830..868
FT                   /note="EGF-like 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          869..910
FT                   /note="EGF-like 7; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          911..951
FT                   /note="EGF-like 8; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          970..1011
FT                   /note="EGF-like 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REGION          1065..1084
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1113..1135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        148
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        321
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        401
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        814
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        851
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        925
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        934
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        316..327
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        322..336
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        338..351
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        357..368
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        364..377
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        379..392
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        398..409
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        405..418
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        420..433
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        436..448
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        444..458
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        460..473
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        742..753
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        749..762
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        764..777
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        834..845
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        839..854
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        856..867
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        873..887
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        880..896
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        898..909
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        915..928
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        922..937
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        939..950
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        974..988
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        982..999
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1001..1010
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1210 AA;  133640 MW;  46EABA4C49886003 CRC64;
     MLLFLIILLP VVFKFSFVSL SVLQGWDCSE GSSSGKGNST CVGPEPFLIF SHGGSIFRID
     LDGTNYEQLV ADAGVSVIMD FHYYKERLYW VDLERQLLQR VFLNGTRQET VCNIEKNVSG
     MAINWINEEL IWSNQQEGII TVTDMKGNNS RVLLSALKYP ANVAIDPVER FIFWSSEVAG
     SLHRADLNGV EVKILLETSE RITAVSLDVL DKRLFWIQNN RDGSNSYICS CNYDGGSVHF
     NKHLTQHSLF AMSLFGDRIF YSTWKKKTIW IANKRKDMVR INLNPSFVPP GGTKVVHPLL
     QPKAESDAWA PGQKLCLRKG NCTGSVCEQD SKSHLCTCAE GYTLSPDGKH CEDVNECAFW
     NHGCTLGCEN IPGSYYCTCP VGFILLPDGK RCHQLISCPS NTSKCSHDCV LTSDGPICFC
     PEGSVLETDG KTCSGCSSPD NGGCSQLCLP LSPVSWECGC FPGYDLQLDK KSCAASGPQP
     FLLFANSQDI RHVRFDGTDY GSLLSQQMGM VFALDHDPVE NKIYFAHTAL KWIERANMDG
     SQRERLIEEA VDVPEGLAID WIDRKFYWTD RGKALIEGSD LNGKHREIII KEEVSQPRGI
     AVHPMAKRLF WTDMGINPRI ESSSLQGIGR RVIASSDLVW PSGITIDYLT DKLYWCDAKQ
     SVIEMANLDG SKRQRLAQND VGHPFAIAVF EDHVWFSDWT MPSVIRVNKR TGKNRVRLRG
     SMLKPSSLVV VHPLAKPGSD PCLHQNGGCE HICKERFGSA QCLCREGFVK APDGKMCLAL
     NGHQIPPAVG SEADLSNQVT PLDVLSRNRG SEDNSTESQH MLVAEIMVSD NDDCGPIRCG
     TWGQCVSEGE NATCQCLKGF TGDGKLCSDI NECGTSTTVC PPTSSKCINT EGGYVCQCSE
     GYRGDGIHCL DIDECQLGIH TCGENATCTN TEGNYTCMCA GTLSEPGQMC PDSTPPSVLM
     EDGRYSVRNS YQECPPSYDG YCLYNGVCMY IEAVDRYACN CVFGYVGERC QHRDLKWELR
     HAGQGRQRQV TVVAVCVVAL VLLLLLGLWG AHCYRTKKLP SKNLKNPYEE SSREVSRPTD
     SEAGMASCPQ PWFVVIKEHQ NLRNGSQSMA LKDSEAADVS QFSSRETGSV QLPSRRNEPQ
     VYMGAEQGCC IPPSSDKGPG PHGMQWGFHL PSCEAQPIAL GVEKSQSLLS ANPILQQRAS
     DLPHQKKLTQ
 
 
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