GIMA4_RAT
ID GIMA4_RAT Reviewed; 310 AA.
AC Q8K3K9;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=GTPase IMAP family member 4;
DE AltName: Full=Immunity-associated nucleotide 1 protein;
DE Short=IAN-1;
DE AltName: Full=Immunity-associated protein 4;
GN Name=Gimap4; Synonyms=Ian1 {ECO:0000303|PubMed:12031988}, Imap4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-55, AND TISSUE SPECIFICITY.
RC STRAIN=BB; TISSUE=Thymus;
RX PubMed=12031988; DOI=10.2337/diabetes.51.6.1972;
RA Hornum L., Romer J., Markholst H.;
RT "The diabetes-prone BB rat carries a frameshift mutation in Ian4, a
RT positional candidate of Iddm1.";
RL Diabetes 51:1972-1979(2002).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: During thymocyte development, may play a role in the
CC regulation of apoptosis (By similarity). GTPase which exhibits a higher
CC affinity for GDP than for GTP (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q99JY3}.
CC -!- SUBUNIT: May interact (via IQ domain) with calmodulin/CALM1 only in the
CC absence of Ca(2+) (By similarity). Interacts with BAX, but not with
CC other Bcl-2 family members (By similarity).
CC {ECO:0000250|UniProtKB:Q99JY3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q99JY3}.
CC -!- TISSUE SPECIFICITY: Primarily expressed in spleen, thymus, heart, lung
CC and intestine and, at lower levels, in liver, kidney, stomach and
CC muscle (PubMed:12031988). In the spleen, expressed in periarteriolar
CC lymphatic sheets (PubMed:12031988). In the thymus, detected in the
CC medulla (PubMed:12031988). {ECO:0000269|PubMed:12031988}.
CC -!- PTM: Phosphorylated at very low levels in resting splenocytes. Rapidly
CC and transiently phosphorylated in response to splenocyte activation.
CC {ECO:0000250|UniProtKB:Q99JY3}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. AIG1/Toc34/Toc159-like paraseptin GTPase family.
CC IAN subfamily. {ECO:0000305}.
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DR EMBL; AY070268; AAL59007.1; -; mRNA.
DR RefSeq; NP_775176.2; NM_173153.2.
DR AlphaFoldDB; Q8K3K9; -.
DR SMR; Q8K3K9; -.
DR STRING; 10116.ENSRNOP00000038031; -.
DR iPTMnet; Q8K3K9; -.
DR PhosphoSitePlus; Q8K3K9; -.
DR PaxDb; Q8K3K9; -.
DR PRIDE; Q8K3K9; -.
DR GeneID; 286938; -.
DR KEGG; rno:286938; -.
DR UCSC; RGD:628765; rat.
DR CTD; 55303; -.
DR RGD; 628765; Gimap4.
DR eggNOG; ENOG502R7PE; Eukaryota.
DR InParanoid; Q8K3K9; -.
DR OrthoDB; 1092873at2759; -.
DR PhylomeDB; Q8K3K9; -.
DR PRO; PR:Q8K3K9; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006703; G_AIG1.
DR InterPro; IPR045058; GIMA/IAN/Toc.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10903; PTHR10903; 1.
DR Pfam; PF04548; AIG1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51720; G_AIG1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; GTP-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..310
FT /note="GTPase IMAP family member 4"
FT /id="PRO_0000190989"
FT DOMAIN 28..230
FT /note="AIG1-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT DOMAIN 233..262
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..44
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 64..68
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 85..88
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 154..157
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 190..192
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT COILED 239..297
FT /evidence="ECO:0000255"
FT COMPBIAS 8..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 37..45
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NUV9"
FT BINDING 58
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NUV9"
FT BINDING 155..157
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NUV9"
FT BINDING 191
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NUV9"
FT VARIANT 55
FT /note="A -> V"
FT /evidence="ECO:0000269|PubMed:12031988"
SQ SEQUENCE 310 AA; 35823 MW; 2EDF156D559C0DAE CRC64;
MEAQYSGVGS IPENSRSSHE LGIQDQGSPQ LRIVLLGKTG AGKSSTGNSI LGRKAFLSGI
CAKSITKVCE KGVSIWDGKE LVVVDTPGIF DTEVPDADTQ KEITRCVALT SPGPHALLLV
IPLGCYTVEE HKATRKLLSM FEKKARRFMI LLLTRKDDLE DTDIHEYLET APEVLQELIY
EFRNRYCLFN NKASGAEQEE QKRQLLTLVQ SMVRENGGKY FTNKMYESAE GVIQKQTWKK
KEFYREELER ERARIRREYE AEIQDLRDEL ERERRRARME REFNENELIF AERQQNARRE
VENTSMIYLN
