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ATT_APLCA
ID   ATT_APLCA               Reviewed;          76 AA.
AC   O96910;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Attractin;
DE   Flags: Precursor;
GN   Name=ATT;
OS   Aplysia californica (California sea hare).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC   Aplysiidae; Aplysia.
OX   NCBI_TaxID=6500;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Albumen gland;
RX   PubMed=9379840; DOI=10.1016/s0169-328x(97)00154-x;
RA   Fan X., Wu B., Nagle G.T., Painter S.D.;
RT   "Molecular cloning of a cDNA encoding a potential water-borne pheromonal
RT   attractant released during Aplysia egg laying.";
RL   Brain Res. Mol. Brain Res. 48:167-170(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 19-76, AND MASS SPECTROMETRY.
RC   TISSUE=Albumen gland;
RX   PubMed=9604313; DOI=10.2307/1543042;
RA   Painter S.D., Clough B., Garden R.W., Sweedler J.V., Nagle G.T.;
RT   "Characterization of Aplysia attractin, the first water-borne peptide
RT   pheromone in invertebrates.";
RL   Biol. Bull. 194:120-131(1998).
RN   [3]
RP   FUNCTION.
RX   PubMed=12917218; DOI=10.2307/1543441;
RA   Painter S.D., Clough B., Black S., Nagle G.T.;
RT   "Behavioral characterization of attractin, a water-borne peptide pheromone
RT   in the genus aplysia.";
RL   Biol. Bull. 205:16-25(2003).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH ENTICIN AND TEMPTIN.
RC   TISSUE=Albumen gland;
RX   PubMed=15054104; DOI=10.1074/jbc.m313585200;
RA   Cummins S.F., Nichols A.E., Amare A., Hummon A.B., Sweedler J.V.,
RA   Nagle G.T.;
RT   "Characterization of Aplysia enticin and temptin, two novel water-borne
RT   protein pheromones that act in concert with attractin to stimulate mate
RT   attraction.";
RL   J. Biol. Chem. 279:25614-25622(2004).
RN   [5]
RP   STRUCTURE BY NMR OF 19-76, AND DISULFIDE BONDS.
RX   PubMed=12924946; DOI=10.1021/bi0274322;
RA   Garimella R., Xu Y., Schein C.H., Rajarathnam K., Nagle G.T., Painter S.D.,
RA   Braun W.;
RT   "NMR solution structure of attractin, a water-borne protein pheromone from
RT   the mollusk Aplysia californica.";
RL   Biochemistry 42:9970-9979(2003).
CC   -!- FUNCTION: Water-borne pheromone that attract the marine mollusk Aplysia
CC       into breeding aggregations and coordinate male and female reproductive
CC       behavior within the aggregation. {ECO:0000250,
CC       ECO:0000269|PubMed:12917218, ECO:0000269|PubMed:15054104}.
CC   -!- SUBUNIT: Binds to temptin and enticin.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Produced by the albumen gland of the egg cordons.
CC   -!- MASS SPECTROMETRY: Mass=8058; Mass_error=5; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:9604313};
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DR   EMBL; U85586; AAD00569.1; -; mRNA.
DR   PIR; A59060; A59060.
DR   RefSeq; NP_001191562.1; NM_001204633.1.
DR   PDB; 1T50; NMR; -; A=19-76.
DR   PDBsum; 1T50; -.
DR   AlphaFoldDB; O96910; -.
DR   SMR; O96910; -.
DR   GeneID; 100533337; -.
DR   CTD; 100533337; -.
DR   EvolutionaryTrace; O96910; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0000772; F:mating pheromone activity; IEA:InterPro.
DR   GO; GO:0019953; P:sexual reproduction; IEA:InterPro.
DR   Gene3D; 1.20.1400.10; -; 1.
DR   InterPro; IPR012529; Attractin.
DR   InterPro; IPR036585; Attractin_sf.
DR   Pfam; PF08037; Attractin; 1.
DR   SUPFAM; SSF90183; SSF90183; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Pheromone; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:9604313"
FT   CHAIN           19..76
FT                   /note="Attractin"
FT                   /id="PRO_0000020764"
FT   CARBOHYD        26
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        22..59
FT                   /evidence="ECO:0000269|PubMed:12924946"
FT   DISULFID        31..51
FT                   /evidence="ECO:0000269|PubMed:12924946"
FT   DISULFID        38..44
FT                   /evidence="ECO:0000269|PubMed:12924946"
FT   TURN            24..27
FT                   /evidence="ECO:0007829|PDB:1T50"
FT   HELIX           28..34
FT                   /evidence="ECO:0007829|PDB:1T50"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:1T50"
FT   TURN            41..43
FT                   /evidence="ECO:0007829|PDB:1T50"
FT   HELIX           48..56
FT                   /evidence="ECO:0007829|PDB:1T50"
FT   HELIX           57..59
FT                   /evidence="ECO:0007829|PDB:1T50"
FT   HELIX           60..63
FT                   /evidence="ECO:0007829|PDB:1T50"
FT   STRAND          68..71
FT                   /evidence="ECO:0007829|PDB:1T50"
SQ   SEQUENCE   76 AA;  8181 MW;  47924BFC98B9C69C CRC64;
     MKVAIIILSL ALVAAVFADQ NCDIGNITSQ CQMQHKNCED ANGCDTIIEE CKTSMVERCQ
     NQEFESAAGS TTLGPQ
 
 
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