GIMA5_HUMAN
ID GIMA5_HUMAN Reviewed; 307 AA.
AC Q96F15; D3DWZ5; Q6IA75; Q96NE4; Q9NUK9;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=GTPase IMAP family member 5;
DE AltName: Full=Immune-associated nucleotide-binding protein 5;
DE AltName: Full=Immunity-associated nucleotide 4-like 1 protein;
DE AltName: Full=Immunity-associated nucleotide 5 protein;
DE Short=IAN-5;
DE Short=hIAN5 {ECO:0000303|PubMed:14724691};
DE AltName: Full=Immunity-associated protein 3;
GN Name=GIMAP5; Synonyms=IAN4L1, IAN5, IMAP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Histiocytic lymphoma;
RX PubMed=14724691; DOI=10.1038/sj.gene.6364044;
RA Zenz T., Roessner A., Thomas A., Froehling S., Doehner H., Calabretta B.,
RA Daheron L.;
RT "hIan5: the human ortholog to the rat Ian4/Iddm1/lyp is a new member of the
RT Ian family that is overexpressed in B-cell lymphoid malignancies.";
RL Genes Immun. 5:109-116(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH BAD; BAK1; BAX; BCL2L1 AND BCL2L11.
RX PubMed=16509771; DOI=10.1371/journal.pbio.0040103;
RA Nitta T., Nasreen M., Seike T., Goji A., Ohigashi I., Miyazaki T., Ohta T.,
RA Kanno M., Takahama Y.;
RT "IAN family critically regulates survival and development of T
RT lymphocytes.";
RL PLoS Biol. 4:593-605(2006).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=21487483; DOI=10.4161/self.1.3.12819;
RA Wong V.W., Saunders A.E., Hutchings A., Pascall J.C., Carter C.,
RA Bright N.A., Walker S.A., Ktistakis N.T., Butcher G.W.;
RT "The autoimmunity-related GIMAP5 GTPase is a lysosome-associated protein.";
RL Self/Nonself 1:259-268(2010).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT PRO-204, AND
RP CHARACTERIZATION OF VARIANT PRO-204.
RX PubMed=29382851; DOI=10.1038/s41467-018-02897-7;
RA Patterson A.R., Endale M., Lampe K., Aksoylar H.I., Flagg A.,
RA Woodgett J.R., Hildeman D., Jordan M.B., Singh H., Kucuk Z., Bleesing J.,
RA Hoebe K.;
RT "Gimap5-dependent inactivation of GSK3beta is required for CD4+ T cell
RT homeostasis and prevention of immune pathology.";
RL Nat. Commun. 9:430-430(2018).
RN [9]
RP VARIANTS NCPH2 THR-47; LEU-109; PRO-204 AND PHE-223, AND INVOLVEMENT IN
RP NCPH2.
RX PubMed=33956074; DOI=10.1084/jem.20201745;
RA Drzewiecki K., Choi J., Brancale J., Leney-Greene M.A., Sari S., Dalgic B.,
RA Uenluesoy Aksu A., Evirgen Sahin G., Ozen A., Baris S., Karakoc-Aydiner E.,
RA Jain D., Kleiner D., Schmalz M., Radhakrishnan K., Zhang J., Hoebe K.,
RA Su H.C., Pereira J.P., Lenardo M.J., Lifton R.P., Vilarinho S.;
RT "GIMAP5 maintains liver endothelial cell homeostasis and prevents portal
RT hypertension.";
RL J. Exp. Med. 218:0-0(2021).
CC -!- FUNCTION: Plays a role in T lymphocyte development and the optimal
CC generation of CD4/CD8 double-positive thymocytes (By similarity).
CC Inhibitor of GSK3A, possibly by sequestering GSK3A in cytoplasmic
CC vesicles and impairing its translocation to the nucleus. Consequently,
CC impairs GSK3A-dependent transcriptional program and regulation of the
CC DNA damage response occurring during T cells proliferation
CC (PubMed:29382851). Required for the survival of peripheral T cells,
CC natural killer (NK) and NK T-cell development and the maintenance of
CC normal liver function (By similarity). May promote the survival of
CC mature T lymphocytes upon cytokine withdrawal (By similarity). May
CC regulate Ca(2+) homeostasis by modulating lysosomal Ca(2+) stores,
CC preventing its accumulation in the absence of T cell activation (By
CC similarity). May play a role in mitochondrial DNA segregation in
CC hematopoietic tissues (By similarity). Is a regulator of liver
CC endothelial cell homeostasis (By similarity).
CC {ECO:0000250|UniProtKB:Q8BWF2, ECO:0000250|UniProtKB:Q8K3L6,
CC ECO:0000269|PubMed:29382851}.
CC -!- SUBUNIT: Interacts with BAD, BAK1, BAX, BCL2, BCL2L1/Bcl-xL and
CC BCL2L11/BimEL (PubMed:16509771). The interaction with BAX is increased,
CC when cells initiate apoptosis upon IL2 withdrawal (PubMed:16509771).
CC Also interacts with BCL2 (By similarity). Forms a complex with BCL2L1
CC or MCL1 and HSPA8/HSC70; the interaction between HSPA8 and BCL2L1 or
CC MCL1 is impaired in the absence of GIMAP5 (By similarity). May interact
CC (via N-terminus) with microtubules (By similarity).
CC {ECO:0000250|UniProtKB:Q8BWF2, ECO:0000250|UniProtKB:Q8K3L6,
CC ECO:0000269|PubMed:16509771}.
CC -!- INTERACTION:
CC Q96F15; Q86Y34: ADGRG3; NbExp=3; IntAct=EBI-6166686, EBI-17979264;
CC Q96F15; Q92482: AQP3; NbExp=3; IntAct=EBI-6166686, EBI-2808854;
CC Q96F15; Q13520: AQP6; NbExp=3; IntAct=EBI-6166686, EBI-13059134;
CC Q96F15; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-6166686, EBI-11343438;
CC Q96F15; Q6UXG8-3: BTNL9; NbExp=3; IntAct=EBI-6166686, EBI-17953245;
CC Q96F15; P20138: CD33; NbExp=3; IntAct=EBI-6166686, EBI-3906571;
CC Q96F15; P19397: CD53; NbExp=3; IntAct=EBI-6166686, EBI-6657396;
CC Q96F15; O95471: CLDN7; NbExp=3; IntAct=EBI-6166686, EBI-740744;
CC Q96F15; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-6166686, EBI-6942903;
CC Q96F15; P49447: CYB561; NbExp=3; IntAct=EBI-6166686, EBI-8646596;
CC Q96F15; Q53TN4: CYBRD1; NbExp=3; IntAct=EBI-6166686, EBI-8637742;
CC Q96F15; Q9UBT3: DKK4; NbExp=3; IntAct=EBI-6166686, EBI-18030204;
CC Q96F15; Q15125: EBP; NbExp=3; IntAct=EBI-6166686, EBI-3915253;
CC Q96F15; Q92838: EDA; NbExp=6; IntAct=EBI-6166686, EBI-529425;
CC Q96F15; Q9HAV5: EDA2R; NbExp=3; IntAct=EBI-6166686, EBI-526033;
CC Q96F15; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-6166686, EBI-18535450;
CC Q96F15; P54849: EMP1; NbExp=3; IntAct=EBI-6166686, EBI-4319440;
CC Q96F15; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-6166686, EBI-781551;
CC Q96F15; P34910-2: EVI2B; NbExp=3; IntAct=EBI-6166686, EBI-17640610;
CC Q96F15; Q8TBP5: FAM174A; NbExp=3; IntAct=EBI-6166686, EBI-18636064;
CC Q96F15; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-6166686, EBI-18938272;
CC Q96F15; Q969F0: FATE1; NbExp=3; IntAct=EBI-6166686, EBI-743099;
CC Q96F15; P48165: GJA8; NbExp=3; IntAct=EBI-6166686, EBI-17458373;
CC Q96F15; O75712: GJB3; NbExp=3; IntAct=EBI-6166686, EBI-3908586;
CC Q96F15; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-6166686, EBI-3917143;
CC Q96F15; Q96HH9: GRAMD2B; NbExp=3; IntAct=EBI-6166686, EBI-2832937;
CC Q96F15; P38484: IFNGR2; NbExp=3; IntAct=EBI-6166686, EBI-3905457;
CC Q96F15; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-6166686, EBI-10266796;
CC Q96F15; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-6166686, EBI-749265;
CC Q96F15; Q8N743: KIR3DL3; NbExp=3; IntAct=EBI-6166686, EBI-17272405;
CC Q96F15; Q6UX15-2: LAYN; NbExp=3; IntAct=EBI-6166686, EBI-19944128;
CC Q96F15; Q5T700: LDLRAD1; NbExp=6; IntAct=EBI-6166686, EBI-10173166;
CC Q96F15; Q8N112: LSMEM2; NbExp=6; IntAct=EBI-6166686, EBI-10264855;
CC Q96F15; P20645: M6PR; NbExp=3; IntAct=EBI-6166686, EBI-2907262;
CC Q96F15; Q99735: MGST2; NbExp=3; IntAct=EBI-6166686, EBI-11324706;
CC Q96F15; O14880: MGST3; NbExp=3; IntAct=EBI-6166686, EBI-724754;
CC Q96F15; Q7Z6M3: MILR1; NbExp=3; IntAct=EBI-6166686, EBI-18391669;
CC Q96F15; Q96JA4: MS4A14; NbExp=3; IntAct=EBI-6166686, EBI-12839612;
CC Q96F15; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-6166686, EBI-716063;
CC Q96F15; O14684: PTGES; NbExp=3; IntAct=EBI-6166686, EBI-11161398;
CC Q96F15; Q86VR2: RETREG3; NbExp=5; IntAct=EBI-6166686, EBI-10192441;
CC Q96F15; Q6P5S7: RNASEK; NbExp=3; IntAct=EBI-6166686, EBI-18397230;
CC Q96F15; Q6ZMZ0: RNF19B; NbExp=3; IntAct=EBI-6166686, EBI-2466594;
CC Q96F15; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-6166686, EBI-17247926;
CC Q96F15; Q3SXP7: SHISAL1; NbExp=3; IntAct=EBI-6166686, EBI-18037857;
CC Q96F15; Q14973: SLC10A1; NbExp=3; IntAct=EBI-6166686, EBI-3923031;
CC Q96F15; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-6166686, EBI-17295964;
CC Q96F15; Q9BZL3: SMIM3; NbExp=3; IntAct=EBI-6166686, EBI-741850;
CC Q96F15; Q9HBV2: SPACA1; NbExp=3; IntAct=EBI-6166686, EBI-17498703;
CC Q96F15; P27105: STOM; NbExp=3; IntAct=EBI-6166686, EBI-1211440;
CC Q96F15; Q16623: STX1A; NbExp=3; IntAct=EBI-6166686, EBI-712466;
CC Q96F15; P32856-2: STX2; NbExp=3; IntAct=EBI-6166686, EBI-11956649;
CC Q96F15; Q12846: STX4; NbExp=3; IntAct=EBI-6166686, EBI-744942;
CC Q96F15; P21579: SYT1; NbExp=3; IntAct=EBI-6166686, EBI-524909;
CC Q96F15; Q96CE8: TM4SF18; NbExp=3; IntAct=EBI-6166686, EBI-13351685;
CC Q96F15; Q96DZ7: TM4SF19; NbExp=3; IntAct=EBI-6166686, EBI-6448756;
CC Q96F15; Q9H3N1: TMX1; NbExp=3; IntAct=EBI-6166686, EBI-1051115;
CC Q96F15; Q9Y320: TMX2; NbExp=3; IntAct=EBI-6166686, EBI-6447886;
CC Q96F15; Q9NS68-2: TNFRSF19; NbExp=3; IntAct=EBI-6166686, EBI-12089038;
CC Q96F15; Q8WUV1: TSPAN18; NbExp=3; IntAct=EBI-6166686, EBI-17670824;
CC Q96F15; Q5T4F4: ZFYVE27; NbExp=3; IntAct=EBI-6166686, EBI-3892947;
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:21487483,
CC ECO:0000269|PubMed:29382851}; Single-pass type IV membrane protein
CC {ECO:0000305}. Endosome, multivesicular body membrane
CC {ECO:0000269|PubMed:21487483}; Single-pass type IV membrane protein
CC {ECO:0000305}. Endosome membrane {ECO:0000250|UniProtKB:Q8K3L6};
CC Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q8K3L6}.
CC Note=The mitochondrial localization originally reported was observed
CC with C-terminally tagged protein and was not confirmed in later
CC publications. {ECO:0000305|PubMed:14724691,
CC ECO:0000305|PubMed:21487483}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96F15-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96F15-2; Sequence=VSP_008961;
CC -!- TISSUE SPECIFICITY: Widely expressed with high levels in lymph node and
CC spleen (PubMed:14724691). High expression found in T lymphocytes,
CC including CD4 and CD8-positive T-cells, and monocytes (PubMed:14724691,
CC PubMed:29382851). Very low expression levels in B-lymphocytes
CC (PubMed:14724691). {ECO:0000269|PubMed:14724691,
CC ECO:0000269|PubMed:29382851}.
CC -!- DISEASE: Portal hypertension, non-cirrhotic, 2 (NCPH2) [MIM:619463]: An
CC autosomal recessive disorder characterized by portal hypertension
CC associated with hepatosplenomegaly, in absence of cirrhosis. Portal
CC hypertension is defined by a portal venous system pressure that is at
CC least 5 mm Hg higher than the pressure in the inferior vena cava. High
CC pressure in the portal venous system leads to shunting of blood through
CC vessels that are poorly suited to carrying large blood volumes,
CC resulting in collateral circulation and splenomegaly. NCPH2 patients
CC have jaundice, hyperbilirubinemia, pancytopenia, including neutropenia,
CC lymphopenia, and thrombocytopenia, hepatosplenomegaly, and esophageal
CC varices. Some patients may have recurrent infections or features
CC suggestive of an immunodeficiency. {ECO:0000269|PubMed:33956074}.
CC Note=The disease may be caused by variants affecting the gene
CC represented in this entry.
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; AK002158; BAA92115.1; -; mRNA.
DR EMBL; AK055568; BAB70958.1; -; mRNA.
DR EMBL; CR457280; CAG33561.1; -; mRNA.
DR EMBL; CH471173; EAW54092.1; -; Genomic_DNA.
DR EMBL; CH471173; EAW54093.1; -; Genomic_DNA.
DR EMBL; CH471173; EAW54094.1; -; Genomic_DNA.
DR EMBL; BC011732; AAH11732.1; -; mRNA.
DR CCDS; CCDS5907.1; -. [Q96F15-1]
DR RefSeq; NP_060854.2; NM_018384.4. [Q96F15-1]
DR PDB; 6Z3E; X-ray; 2.80 A; A=1-276.
DR PDBsum; 6Z3E; -.
DR AlphaFoldDB; Q96F15; -.
DR SMR; Q96F15; -.
DR BioGRID; 120621; 71.
DR DIP; DIP-59484N; -.
DR IntAct; Q96F15; 62.
DR iPTMnet; Q96F15; -.
DR PhosphoSitePlus; Q96F15; -.
DR BioMuta; GIMAP5; -.
DR DMDM; 38372381; -.
DR jPOST; Q96F15; -.
DR MassIVE; Q96F15; -.
DR MaxQB; Q96F15; -.
DR PaxDb; Q96F15; -.
DR PeptideAtlas; Q96F15; -.
DR PRIDE; Q96F15; -.
DR ProteomicsDB; 76484; -. [Q96F15-1]
DR ProteomicsDB; 76485; -. [Q96F15-2]
DR Antibodypedia; 2723; 184 antibodies from 27 providers.
DR DNASU; 55340; -.
DR Ensembl; ENST00000358647.5; ENSP00000351473.3; ENSG00000196329.12. [Q96F15-1]
DR Ensembl; ENST00000498181.6; ENSP00000487840.2; ENSG00000196329.12. [Q96F15-1]
DR GeneID; 55340; -.
DR KEGG; hsa:55340; -.
DR MANE-Select; ENST00000358647.5; ENSP00000351473.3; NM_018384.5; NP_060854.2.
DR UCSC; uc003whr.3; human. [Q96F15-1]
DR CTD; 55340; -.
DR DisGeNET; 55340; -.
DR GeneCards; GIMAP5; -.
DR HGNC; HGNC:18005; GIMAP5.
DR HPA; ENSG00000196329; Tissue enhanced (lymphoid).
DR MIM; 608086; gene.
DR MIM; 619463; phenotype.
DR neXtProt; NX_Q96F15; -.
DR OpenTargets; ENSG00000196329; -.
DR PharmGKB; PA29578; -.
DR VEuPathDB; HostDB:ENSG00000196329; -.
DR eggNOG; ENOG502RB0C; Eukaryota.
DR GeneTree; ENSGT00940000154844; -.
DR HOGENOM; CLU_010468_1_1_1; -.
DR InParanoid; Q96F15; -.
DR PhylomeDB; Q96F15; -.
DR TreeFam; TF330845; -.
DR PathwayCommons; Q96F15; -.
DR SignaLink; Q96F15; -.
DR BioGRID-ORCS; 55340; 9 hits in 1065 CRISPR screens.
DR GeneWiki; GIMAP5; -.
DR GenomeRNAi; 55340; -.
DR Pharos; Q96F15; Tbio.
DR PRO; PR:Q96F15; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q96F15; protein.
DR Bgee; ENSG00000196329; Expressed in right lung and 92 other tissues.
DR ExpressionAtlas; Q96F15; baseline and differential.
DR Genevisible; Q96F15; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
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 3D-structure; Alternative splicing; Endosome; GTP-binding; Lysosome;
KW Membrane; Nucleotide-binding; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..307
FT /note="GTPase IMAP family member 5"
FT /id="PRO_0000190990"
FT TOPO_DOM 1..284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..307
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 25..228
FT /note="AIG1-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 34..42
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8WWP7"
FT BINDING 55
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UG22"
FT BINDING 152..154
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8WWP7"
FT BINDING 189
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8WWP7"
FT VAR_SEQ 1..14
FT /note="MGGFQRGKYGTMAE -> MQDSPIVVCTLLCTHKYVYHSGEDVHSFHEITMN
FT NDLTVLRIINLVRYKTSFST (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008961"
FT VARIANT 47
FT /note="I -> T (in NCPH2; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33956074"
FT /id="VAR_086141"
FT VARIANT 109
FT /note="P -> L (in NCPH2; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33956074"
FT /id="VAR_086142"
FT VARIANT 204
FT /note="L -> P (in NCPH2; unknown pathological significance;
FT strong decrease in protein level; dbSNP:rs72650695)"
FT /evidence="ECO:0000269|PubMed:29382851,
FT ECO:0000269|PubMed:33956074"
FT /id="VAR_081683"
FT VARIANT 223
FT /note="L -> F (in NCPH2; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33956074"
FT /id="VAR_086143"
FT CONFLICT 174
FT /note="K -> E (in Ref. 2; BAA92115)"
FT /evidence="ECO:0000305"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:6Z3E"
FT HELIX 40..48
FT /evidence="ECO:0007829|PDB:6Z3E"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:6Z3E"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:6Z3E"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:6Z3E"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:6Z3E"
FT HELIX 94..107
FT /evidence="ECO:0007829|PDB:6Z3E"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:6Z3E"
FT HELIX 125..138
FT /evidence="ECO:0007829|PDB:6Z3E"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:6Z3E"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:6Z3E"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:6Z3E"
FT HELIX 161..167
FT /evidence="ECO:0007829|PDB:6Z3E"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:6Z3E"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:6Z3E"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:6Z3E"
FT HELIX 193..213
FT /evidence="ECO:0007829|PDB:6Z3E"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:6Z3E"
FT HELIX 222..231
FT /evidence="ECO:0007829|PDB:6Z3E"
FT HELIX 242..261
FT /evidence="ECO:0007829|PDB:6Z3E"
SQ SEQUENCE 307 AA; 34846 MW; D219F52DE910C5BA CRC64;
MGGFQRGKYG TMAEGRSEDN LSATPPALRI ILVGKTGCGK SATGNSILGQ PVFESKLRAQ
SVTRTCQVKT GTWNGRKVLV VDTPSIFESQ ADTQELYKNI GDCYLLSAPG PHVLLLVIQL
GRFTAQDTVA IRKVKEVFGT GAMRHVVILF THKEDLGGQA LDDYVANTDN CSLKDLVREC
ERRYCAFNNW GSVEEQRQQQ AELLAVIERL GREREGSFHS NDLFLDAQLL QRTGAGACQE
DYRQYQAKVE WQVEKHKQEL RENESNWAYK ALLRVKHLML LHYEIFVFLL LCSILFFIIF
LFIFHYI