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NEU2_ONCKE
ID   NEU2_ONCKE              Reviewed;         156 AA.
AC   Q91167;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Isotocin-neurophysin IT 2;
DE   Contains:
DE     RecName: Full=Isotocin;
DE              Short=IT;
DE   Contains:
DE     RecName: Full=Neurophysin IT 2;
DE   Flags: Precursor;
OS   Oncorhynchus keta (Chum salmon) (Salmo keta).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8018;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Tsugaruishi; TISSUE=Brain;
RX   PubMed=2045542; DOI=10.1007/bf00571256;
RA   Hyodo S., Kato Y., Ono M., Urano A.;
RT   "Cloning and sequence analyses of cDNAs encoding vasotocin and isotocin
RT   precursors of chum salmon, Oncorhynchus keta: evolutionary relationships of
RT   neurohypophysial hormone precursors.";
RL   J. Comp. Physiol. B 160:601-608(1991).
CC   -!- FUNCTION: Isotocin causes contraction of smooth muscles.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Seven disulfide bonds are present in neurophysin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the vasopressin/oxytocin family. {ECO:0000305}.
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DR   EMBL; D10941; BAA01735.1; -; mRNA.
DR   PIR; JC1490; JC1490.
DR   AlphaFoldDB; Q91167; -.
DR   SMR; Q91167; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005185; F:neurohypophyseal hormone activity; IEA:InterPro.
DR   Gene3D; 2.60.9.10; -; 1.
DR   InterPro; IPR000981; Neurhyp_horm.
DR   InterPro; IPR036387; Neurhyp_horm_dom_sf.
DR   InterPro; IPR022423; Neurohypophysial_hormone_CS.
DR   PANTHER; PTHR11681; PTHR11681; 1.
DR   Pfam; PF00184; Hormone_5; 1.
DR   PIRSF; PIRSF001815; Nonapeptide_hormone_precursor; 1.
DR   PRINTS; PR00831; NEUROPHYSIN.
DR   SMART; SM00003; NH; 1.
DR   SUPFAM; SSF49606; SSF49606; 1.
DR   PROSITE; PS00264; NEUROHYPOPHYS_HORM; 1.
PE   2: Evidence at transcript level;
KW   Amidation; Cleavage on pair of basic residues; Disulfide bond; Hormone;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   PEPTIDE         20..28
FT                   /note="Isotocin"
FT                   /id="PRO_0000020562"
FT   CHAIN           32..156
FT                   /note="Neurophysin IT 2"
FT                   /id="PRO_0000020563"
FT   MOD_RES         28
FT                   /note="Glycine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        20..25
FT                   /evidence="ECO:0000250|UniProtKB:P01175"
FT   DISULFID        41..85
FT                   /evidence="ECO:0000250|UniProtKB:P01175"
FT   DISULFID        44..58
FT                   /evidence="ECO:0000250|UniProtKB:P01175"
FT   DISULFID        52..75
FT                   /evidence="ECO:0000250|UniProtKB:P01175"
FT   DISULFID        59..65
FT                   /evidence="ECO:0000250|UniProtKB:P01175"
FT   DISULFID        92..105
FT                   /evidence="ECO:0000250|UniProtKB:P01175"
FT   DISULFID        99..117
FT                   /evidence="ECO:0000250|UniProtKB:P01175"
FT   DISULFID        106..111
FT                   /evidence="ECO:0000250|UniProtKB:P01175"
SQ   SEQUENCE   156 AA;  16352 MW;  23717F951CFB1914 CRC64;
     MTGAAVSVCL LYALSVCSAC YISNCPIGGK RSIMDAPQRK CMSCGPGEQG RCFGPSICCG
     KDVGCWMGSP ETAHCMEENY LPTPCQVGGR PCGSDTVRCA SPGVCCDSEG CSADQSCFAE
     EEGDNQIGQS EGSNSADVIL RLLHLADHTP PHRVHQ
 
 
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