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FP2_MYTGA
ID   FP2_MYTGA               Reviewed;         473 AA.
AC   Q25464;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Adhesive plaque matrix protein 2;
DE   AltName: Full=Foot protein 2;
DE   AltName: Full=MGFP-2;
DE            Short=MGFP2;
DE   Flags: Precursor;
GN   Name=FP2;
OS   Mytilus galloprovincialis (Mediterranean mussel).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae;
OC   Mytilus.
OX   NCBI_TaxID=29158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Foot;
RX   PubMed=7896812; DOI=10.1074/jbc.270.12.6698;
RA   Inoue K., Takeuchi Y., Miki D., Odo S.;
RT   "Mussel adhesive plaque protein gene is a novel member of epidermal growth
RT   factor-like gene family.";
RL   J. Biol. Chem. 270:6698-6701(1995).
CC   -!- FUNCTION: Provides adhesiveness to the mussel's foot. Mussels produce
CC       one of the strongest water insoluble glues. The mussel's adhesive is a
CC       bundle of threads, called a byssus, formed by a fibrous collagenous
CC       core coated with adhesive proteins.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Produced by the byssal gland.
CC   -!- DEVELOPMENTAL STAGE: Expression starts at the pediveliger, foot
CC       formation, stage.
CC   -!- PTM: Contains L-DOPA (3',4'-dihydroxyphenylalanine). {ECO:0000250}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Sticky business - Issue 2 of
CC       September 2001;
CC       URL="https://web.expasy.org/spotlight/back_issues/002";
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DR   EMBL; D43794; BAA07852.1; -; mRNA.
DR   PIR; A56175; A56175.
DR   AlphaFoldDB; Q25464; -.
DR   SMR; Q25464; -.
DR   PRIDE; Q25464; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   Pfam; PF00008; EGF; 7.
DR   SMART; SM00181; EGF; 11.
DR   SMART; SM00179; EGF_CA; 10.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS00022; EGF_1; 11.
DR   PROSITE; PS01186; EGF_2; 10.
DR   PROSITE; PS50026; EGF_3; 11.
PE   2: Evidence at transcript level;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Hydroxylation; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..473
FT                   /note="Adhesive plaque matrix protein 2"
FT                   /id="PRO_0000007588"
FT   DOMAIN          45..81
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          82..117
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          118..154
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          155..191
FT                   /note="EGF-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          192..228
FT                   /note="EGF-like 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          229..265
FT                   /note="EGF-like 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          266..301
FT                   /note="EGF-like 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          302..340
FT                   /note="EGF-like 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          342..378
FT                   /note="EGF-like 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          383..420
FT                   /note="EGF-like 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          425..461
FT                   /note="EGF-like 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   MOD_RES         23
FT                   /note="3',4'-dihydroxyphenylalanine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         31
FT                   /note="3',4'-dihydroxyphenylalanine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         36
FT                   /note="3',4'-dihydroxyphenylalanine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         43
FT                   /note="3',4'-dihydroxyphenylalanine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        49..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        54..69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        71..80
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        86..97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        91..106
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        108..117
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        122..133
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        127..143
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        145..154
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        159..170
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        164..180
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        182..191
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        196..207
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        201..217
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        219..228
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        233..244
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        238..254
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        256..265
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        270..281
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        275..290
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        292..301
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        306..317
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        311..328
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        330..339
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        346..357
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        351..366
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        368..377
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        387..399
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        393..408
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        410..419
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        429..440
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        434..449
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        451..460
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   473 AA;  51772 MW;  BA76BA8C3BA49A0F CRC64;
     MLFSFFLLLT CTQLCLGTNR PDYNDDEEDD YKPPVYKPSP SKYRPVNPCL KKPCKYNGVC
     KPRGGSYKCF CKGGYYGYNC NLKNACKPNQ CKNKSRCVPV GKTFKCVCRN GNFGRLCEKN
     VCSPNPCKNN GKCSPLGKTG YKCTCSGGYT GPRCEVHACK PNPCKNKGRC FPDGKTGYKC
     RCVDGYSGPT CQENACKPNP CSNGGTCSAD KFGDYSCECR PGYFGPECER YVCAPNPCKN
     GGICSSDGSG GYRCRCKGGY SGPTCKVNVC KPTPCKNSGR CVNKGSSYNC ICKGGYSGPT
     CGENVCKPNP CQNRGRCYPD NSDDGFKCRC VGGYKGPTCE DKPNPCNTKP CKNGGKCNYN
     GKIYTCKCAY GWRGRHCTDK AYKPNPCVVS KPCKNRGKCI WNGKAYRCKC AYGYGGRHCT
     KKSYKKNPCA SRPCKNRGKC TDKGNGYVCK CARGYSGRYC SLKSPPSYDD DEY
 
 
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