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Database: UniProt
Entry: A0A091E836_FUKDA
LinkDB: A0A091E836_FUKDA
Original site: A0A091E836_FUKDA 
ID   A0A091E836_FUKDA        Unreviewed;       156 AA.
AC   A0A091E836;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=VIP peptide {ECO:0000313|EMBL:KFO31301.1};
GN   ORFNames=H920_07297 {ECO:0000313|EMBL:KFO31301.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO31301.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO31301.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO31301.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: VIP causes vasodilation, lowers arterial blood pressure,
CC       stimulates myocardial contractility, increases glycogenolysis and
CC       relaxes the smooth muscle of trachea, stomach and gall bladder.
CC       {ECO:0000256|ARBA:ARBA00002470}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the glucagon family.
CC       {ECO:0000256|ARBA:ARBA00008369}.
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DR   EMBL; KN122297; KFO31301.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091E836; -.
DR   STRING; 885580.ENSFDAP00000022442; -.
DR   eggNOG; ENOG502QVTA; Eukaryota.
DR   Proteomes; UP000028990; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005184; F:neuropeptide hormone activity; IEA:InterPro.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:UniProt.
DR   GO; GO:0048255; P:mRNA stabilization; ISS:AgBase.
DR   GO; GO:0070459; P:prolactin secretion; ISS:AgBase.
DR   GO; GO:0032879; P:regulation of localization; IEA:UniProt.
DR   Gene3D; 6.10.250.590; -; 2.
DR   InterPro; IPR000532; Glucagon_GIP_secretin_VIP.
DR   InterPro; IPR046963; VIP/GHRH-like.
DR   PANTHER; PTHR11213; GLUCAGON-FAMILY NEUROPEPTIDE; 1.
DR   PANTHER; PTHR11213:SF5; VIP PEPTIDES; 1.
DR   Pfam; PF00123; Hormone_2; 2.
DR   SMART; SM00070; GLUCA; 2.
DR   PROSITE; PS00260; GLUCAGON; 2.
PE   3: Inferred from homology;
KW   Amidation {ECO:0000256|ARBA:ARBA00022815};
KW   Hormone {ECO:0000256|ARBA:ARBA00022702};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..156
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001873877"
FT   DOMAIN          81..103
FT                   /note="Glucagon / GIP / secretin / VIP family"
FT                   /evidence="ECO:0000259|PROSITE:PS00260"
FT   DOMAIN          125..147
FT                   /note="Glucagon / GIP / secretin / VIP family"
FT                   /evidence="ECO:0000259|PROSITE:PS00260"
SQ   SEQUENCE   156 AA;  17757 MW;  8DAF79098F22F210 CRC64;
     MEARSKPQLL VVLTLFSVLF SQTLAWPLFE PPSTLRMDDR VPFEEANEPD PVSLNLDSDI
     LQDALAESDT PYYELSRNSR HADGIFTNDF SKLLGHLSAK KYLESVIGKR VSSNVADRPA
     LTKRHSDAVF TDNYTRLRKQ MAVKKYLNSI LNGKRR
//
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