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AGR2A_XENLA
ID   AGR2A_XENLA             Reviewed;         159 AA.
AC   Q90Y05;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Anterior gradient protein 2-A;
DE            Short=XAgr2 {ECO:0000303|PubMed:12711553};
DE   AltName: Full=Cement gland-specific protein CGS {ECO:0000312|EMBL:AAL26844.1};
DE   Flags: Precursor;
GN   Name=agr2-a; Synonyms=agr2 {ECO:0000303|PubMed:12711553};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAL26844.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Embryo {ECO:0000269|PubMed:12711553};
RX   PubMed=12711553; DOI=10.1016/s1567-133x(02)00077-7;
RA   Novoselov V.V., Alexandrova E.M., Ermakova G.V., Zaraisky A.G.;
RT   "Expression zones of three novel genes abut the developing anterior neural
RT   plate of Xenopus embryo.";
RL   Gene Expr. Patterns 3:225-230(2003).
RN   [2] {ECO:0000312|EMBL:AAI28957.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin {ECO:0000312|EMBL:AAI28957.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Monomer and homodimer. {ECO:0000250|UniProtKB:O95994}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255, ECO:0000305}. Endoplasmic
CC       reticulum {ECO:0000250|UniProtKB:O88312}.
CC   -!- TISSUE SPECIFICITY: Expression begins at the end of gastrulation within
CC       the anterior ectoderm and by the end of neurulation is located within
CC       the cement gland placode. At stage 32 (tailbud), expressed in the cells
CC       surrounding the cement gland and in the otic vesicle. In addition, at
CC       the end of neurulation and afterwards, expressed within the notochord.
CC       {ECO:0000269|PubMed:12711553}.
CC   -!- SIMILARITY: Belongs to the AGR family. {ECO:0000255}.
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DR   EMBL; AF314056; AAL26844.1; -; mRNA.
DR   EMBL; BC128956; AAI28957.1; -; mRNA.
DR   RefSeq; NP_001082165.1; NM_001088696.1.
DR   AlphaFoldDB; Q90Y05; -.
DR   SMR; Q90Y05; -.
DR   DNASU; 398260; -.
DR   GeneID; 398260; -.
DR   KEGG; xla:398260; -.
DR   CTD; 398260; -.
DR   Xenbase; XB-GENE-17332659; agr2.S.
DR   OMA; PTFMITR; -.
DR   OrthoDB; 1382017at2759; -.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 398260; Expressed in internal ear and 16 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISS:UniProtKB.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250|UniProtKB:O95994"
FT   CHAIN           21..159
FT                   /note="Anterior gradient protein 2-A"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000392578"
FT   MOTIF           29..38
FT                   /note="Homodimer stabilization; interchain"
FT                   /evidence="ECO:0000250|UniProtKB:O95994"
FT   MOTIF           44..51
FT                   /note="Homodimer stabilization; interchain"
FT                   /evidence="ECO:0000250|UniProtKB:O95994"
SQ   SEQUENCE   159 AA;  18275 MW;  738D62284838B8EB CRC64;
     METVLKSLFF LLVATSFTLA KERKPQTLSR GWGDNLEWVQ TYEEGLFKAK SENKPLLLIN
     HRNDCPHSQA LKKAFAEHQG IQKLAEEFIL LNVVYDPTDK NLQLDGQYVP KVVFVDPSLV
     VRADLPGKYS NHQYTYEPAD IDHLFENMKK ALVLLKTEL
 
 
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