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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
 
 
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