ID A0A452IVD8_9SAUR Unreviewed; 203 AA.
AC A0A452IVD8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Glucagon / GIP / secretin / VIP family domain-containing protein {ECO:0000259|PROSITE:PS00260};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000032084.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000032084.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 STRING; 38772.ENSGAGP00000032084; -.
DR Ensembl; ENSGAGT00000036379.1; ENSGAGP00000032083.1; ENSGAGG00000022998.1.
DR Ensembl; ENSGAGT00000036380.1; ENSGAGP00000032084.1; ENSGAGG00000022998.1.
DR Ensembl; ENSGAGT00000036381.1; ENSGAGP00000032085.1; ENSGAGG00000022998.1.
DR Ensembl; ENSGAGT00000036382.1; ENSGAGP00000032086.1; ENSGAGG00000022998.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005184; F:neuropeptide hormone activity; IEA:InterPro.
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; 1.
PE 3: Inferred from homology;
KW Amidation {ECO:0000256|ARBA:ARBA00022815};
KW Hormone {ECO:0000256|ARBA:ARBA00022702};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..203
FT /note="Glucagon / GIP / secretin / VIP family domain-
FT containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040596566"
FT DOMAIN 132..154
FT /note="Glucagon / GIP / secretin / VIP family"
FT /evidence="ECO:0000259|PROSITE:PS00260"
FT REGION 44..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 203 AA; 22898 MW; 72CF17A5AD2DD0FA CRC64;
MMEHRSSSQL LLSFTLFSVL CSPALALPPL GTYSAMRLGN RMPFDGASEP NQAQGSLKPE
TDSLQNILPE NDKFYLDMSR ALDRNARHAD GLFTSGYSKL LGQLSARRYL ESLIGKRVSN
NLMDEQMPVK RHSDAVFTDN YSRFRKQMAV KKYLNSVLTG KRSQEELNPA SLRDEAELLE
PSFSETYDDV TVDELLNRLP LSL
//
