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
//