GenomeNet

Database: UniProt
Entry: Q9YHF0_LITPI
LinkDB: Q9YHF0_LITPI
Original site: Q9YHF0_LITPI 
ID   Q9YHF0_LITPI            Unreviewed;       313 AA.
AC   Q9YHF0;
DT   01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=Agrin B19 isoform {ECO:0000313|EMBL:AAC68700.1};
DE   Flags: Fragment;
OS   Lithobates pipiens (Northern leopard frog) (Rana pipiens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=8404 {ECO:0000313|EMBL:AAC68700.1};
RN   [1] {ECO:0000313|EMBL:AAC68700.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:AAC68700.1};
RA   Werle M.J., Jones M.A., Stanco A.M.;
RT   "Agrin produced by Schwann cells does not induce the aggregation of AChRs
RT   at the frog neuromuscular junction.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF096690; AAC68700.1; -; mRNA.
DR   AlphaFoldDB; Q9YHF0; -.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProt.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00110; LamG; 2.
DR   Gene3D; 2.60.120.200; -; 2.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR001791; Laminin_G.
DR   PANTHER; PTHR15036:SF83; AGRIN; 1.
DR   PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00054; Laminin_G_1; 2.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00282; LamG; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}.
FT   DOMAIN          1..142
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          138..176
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          187..313
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DISULFID        166..175
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAC68700.1"
FT   NON_TER         313
FT                   /evidence="ECO:0000313|EMBL:AAC68700.1"
SQ   SEQUENCE   313 AA;  34372 MW;  B31292D1439548F4 CRC64;
     GQKTDAKGDF VSLALHDGHL EYRYDLGKGA AVIRNKEKIP LNTWVSVTLE RNGRKGQMRI
     NNKEQVTGES PKSRKTPHNA LNLKESLYVG GAPDFSKLAR SAAISTSFEG SIQKLNIKGF
     PVLREENILN AIEIATFLGH PCTQKPYPCQ NGGLCIPKKE SYDCVCQRGF SGGQCEKATI
     EKSAGSSEAV SFDGKTYLEY HKVTKNQLTN EIPDHAAAEN PDDPSEKALL TNEFELSIKT
     EATQGLILWS GKGTERSDYI ALAVVGGYVQ MMYDLGSKPV ILRSTVPVNT NQWIRIKALR
     NNRDGILQVG NEA
//
DBGET integrated database retrieval system