Full text data of ELMOD2
ELMOD2
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
ELMO domain-containing protein 2
Note: presumably soluble (membrane word is not in UniProt keywords or features)
ELMO domain-containing protein 2
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q8IZ81
ID ELMD2_HUMAN Reviewed; 293 AA.
AC Q8IZ81; B2R712; D3DNZ0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2003, sequence version 1.
DT 22-JAN-2014, entry version 79.
DE RecName: Full=ELMO domain-containing protein 2;
GN Name=ELMOD2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=16773575; DOI=10.1086/504639;
RA Hodgson U., Pulkkinen V., Dixon M., Peyrard-Janvid M., Rehn M.,
RA Lahermo P., Ollikainen V., Salmenkivi K., Kinnula V., Kere J.,
RA Tukiainen P., Laitinen T.;
RT "ELMOD2 is a candidate gene for familial idiopathic pulmonary
RT fibrosis.";
RL Am. J. Hum. Genet. 79:149-154(2006).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17452337; DOI=10.1074/jbc.M701347200;
RA Bowzard J.B., Cheng D., Peng J., Kahn R.A.;
RT "ELMOD2 is an Arl2 GTPase-activating protein that also acts on Arfs.";
RL J. Biol. Chem. 282:17568-17580(2007).
RN [6]
RP FUNCTION.
RX PubMed=19966137; DOI=10.1096/fj.09-138545;
RA Pulkkinen V., Bruce S., Rintahaka J., Hodgson U., Laitinen T.,
RA Alenius H., Kinnula V.L., Myllaerniemi M., Matikainen S., Kere J.;
RT "ELMOD2, a candidate gene for idiopathic pulmonary fibrosis, regulates
RT antiviral responses.";
RL FASEB J. 24:1167-1177(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Acts as a GTPase-activating protein (GAP) toward guanine
CC nucleotide exchange factors like ARL2, ARL3, ARF1 and ARF6, but
CC not for GTPases outside the Arf family. Regulates IFN-related
CC antiviral responses.
CC -!- TISSUE SPECIFICITY: Alveolar cells (morphologically type II cells)
CC and alveolar macrophages (at protein level). Expressed in brain,
CC colon, heart, kidney, liver, lung, muscle, placenta, small
CC intestine, spleen, stomach and testis. In lung it is expressed in
CC alveolar macrophages and alveolar walls.
CC -!- SIMILARITY: Contains 1 ELMO domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK312800; BAG35659.1; -; mRNA.
DR EMBL; CH471056; EAX05096.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX05097.1; -; Genomic_DNA.
DR EMBL; BC015168; AAH15168.2; -; mRNA.
DR RefSeq; NP_714913.1; NM_153702.3.
DR RefSeq; XP_005262943.1; XM_005262886.1.
DR RefSeq; XP_005262944.1; XM_005262887.1.
DR UniGene; Hs.450105; -.
DR ProteinModelPortal; Q8IZ81; -.
DR IntAct; Q8IZ81; 2.
DR STRING; 9606.ENSP00000326342; -.
DR PhosphoSite; Q8IZ81; -.
DR DMDM; 74728441; -.
DR PaxDb; Q8IZ81; -.
DR PeptideAtlas; Q8IZ81; -.
DR PRIDE; Q8IZ81; -.
DR Ensembl; ENST00000323570; ENSP00000326342; ENSG00000179387.
DR GeneID; 255520; -.
DR KEGG; hsa:255520; -.
DR UCSC; uc003iik.3; human.
DR CTD; 255520; -.
DR GeneCards; GC04P141445; -.
DR HGNC; HGNC:28111; ELMOD2.
DR HPA; HPA047600; -.
DR MIM; 610196; gene.
DR neXtProt; NX_Q8IZ81; -.
DR PharmGKB; PA134984145; -.
DR eggNOG; NOG317117; -.
DR HOGENOM; HOG000007810; -.
DR HOVERGEN; HBG056692; -.
DR InParanoid; Q8IZ81; -.
DR OMA; SFKICMK; -.
DR OrthoDB; EOG712TWN; -.
DR PhylomeDB; Q8IZ81; -.
DR GenomeRNAi; 255520; -.
DR NextBio; 92603; -.
DR PRO; PR:Q8IZ81; -.
DR ArrayExpress; Q8IZ81; -.
DR Bgee; Q8IZ81; -.
DR CleanEx; HS_ELMOD2; -.
DR Genevestigator; Q8IZ81; -.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0006909; P:phagocytosis; IEA:InterPro.
DR GO; GO:0050688; P:regulation of defense response to virus; IDA:UniProtKB.
DR InterPro; IPR006816; Engulfment_cell_motility_ELMO.
DR Pfam; PF04727; ELMO_CED12; 1.
DR PROSITE; PS51335; ELMO; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; Complete proteome; GTPase activation;
KW Reference proteome.
FT CHAIN 1 293 ELMO domain-containing protein 2.
FT /FTId=PRO_0000225017.
FT DOMAIN 126 282 ELMO.
SQ SEQUENCE 293 AA; 34961 MW; 339CD216FC46ADD2 CRC64;
MFISLWEFFY GHFFRFWMKW LLRQMTGKCE LQRIFDTYVG AQRTHRIENS LTYSKNKVLQ
KATHVVQSEV DKYVDDIMKE KNINPEKDAS FKICMKMCLL QITGYKQLYL DVESVRKRPY
DSDNLQHEEL LMKLWNLLMP TKKLNARISK QWAEIGFQGD DPKTDFRGMG ILGLINLVYF
SENYTSEAHQ ILSRSNHPKL GYSYAIVGIN LTEMAYSLLK SEALKFHLYN LVPGIPTMEH
FHQFYCYLVY EFDKFWFEEE PESIMYFNLY REKFHEKIKG LLLDCNVALT LKV
//
ID ELMD2_HUMAN Reviewed; 293 AA.
AC Q8IZ81; B2R712; D3DNZ0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2003, sequence version 1.
DT 22-JAN-2014, entry version 79.
DE RecName: Full=ELMO domain-containing protein 2;
GN Name=ELMOD2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=16773575; DOI=10.1086/504639;
RA Hodgson U., Pulkkinen V., Dixon M., Peyrard-Janvid M., Rehn M.,
RA Lahermo P., Ollikainen V., Salmenkivi K., Kinnula V., Kere J.,
RA Tukiainen P., Laitinen T.;
RT "ELMOD2 is a candidate gene for familial idiopathic pulmonary
RT fibrosis.";
RL Am. J. Hum. Genet. 79:149-154(2006).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17452337; DOI=10.1074/jbc.M701347200;
RA Bowzard J.B., Cheng D., Peng J., Kahn R.A.;
RT "ELMOD2 is an Arl2 GTPase-activating protein that also acts on Arfs.";
RL J. Biol. Chem. 282:17568-17580(2007).
RN [6]
RP FUNCTION.
RX PubMed=19966137; DOI=10.1096/fj.09-138545;
RA Pulkkinen V., Bruce S., Rintahaka J., Hodgson U., Laitinen T.,
RA Alenius H., Kinnula V.L., Myllaerniemi M., Matikainen S., Kere J.;
RT "ELMOD2, a candidate gene for idiopathic pulmonary fibrosis, regulates
RT antiviral responses.";
RL FASEB J. 24:1167-1177(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Acts as a GTPase-activating protein (GAP) toward guanine
CC nucleotide exchange factors like ARL2, ARL3, ARF1 and ARF6, but
CC not for GTPases outside the Arf family. Regulates IFN-related
CC antiviral responses.
CC -!- TISSUE SPECIFICITY: Alveolar cells (morphologically type II cells)
CC and alveolar macrophages (at protein level). Expressed in brain,
CC colon, heart, kidney, liver, lung, muscle, placenta, small
CC intestine, spleen, stomach and testis. In lung it is expressed in
CC alveolar macrophages and alveolar walls.
CC -!- SIMILARITY: Contains 1 ELMO domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK312800; BAG35659.1; -; mRNA.
DR EMBL; CH471056; EAX05096.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX05097.1; -; Genomic_DNA.
DR EMBL; BC015168; AAH15168.2; -; mRNA.
DR RefSeq; NP_714913.1; NM_153702.3.
DR RefSeq; XP_005262943.1; XM_005262886.1.
DR RefSeq; XP_005262944.1; XM_005262887.1.
DR UniGene; Hs.450105; -.
DR ProteinModelPortal; Q8IZ81; -.
DR IntAct; Q8IZ81; 2.
DR STRING; 9606.ENSP00000326342; -.
DR PhosphoSite; Q8IZ81; -.
DR DMDM; 74728441; -.
DR PaxDb; Q8IZ81; -.
DR PeptideAtlas; Q8IZ81; -.
DR PRIDE; Q8IZ81; -.
DR Ensembl; ENST00000323570; ENSP00000326342; ENSG00000179387.
DR GeneID; 255520; -.
DR KEGG; hsa:255520; -.
DR UCSC; uc003iik.3; human.
DR CTD; 255520; -.
DR GeneCards; GC04P141445; -.
DR HGNC; HGNC:28111; ELMOD2.
DR HPA; HPA047600; -.
DR MIM; 610196; gene.
DR neXtProt; NX_Q8IZ81; -.
DR PharmGKB; PA134984145; -.
DR eggNOG; NOG317117; -.
DR HOGENOM; HOG000007810; -.
DR HOVERGEN; HBG056692; -.
DR InParanoid; Q8IZ81; -.
DR OMA; SFKICMK; -.
DR OrthoDB; EOG712TWN; -.
DR PhylomeDB; Q8IZ81; -.
DR GenomeRNAi; 255520; -.
DR NextBio; 92603; -.
DR PRO; PR:Q8IZ81; -.
DR ArrayExpress; Q8IZ81; -.
DR Bgee; Q8IZ81; -.
DR CleanEx; HS_ELMOD2; -.
DR Genevestigator; Q8IZ81; -.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0006909; P:phagocytosis; IEA:InterPro.
DR GO; GO:0050688; P:regulation of defense response to virus; IDA:UniProtKB.
DR InterPro; IPR006816; Engulfment_cell_motility_ELMO.
DR Pfam; PF04727; ELMO_CED12; 1.
DR PROSITE; PS51335; ELMO; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; Complete proteome; GTPase activation;
KW Reference proteome.
FT CHAIN 1 293 ELMO domain-containing protein 2.
FT /FTId=PRO_0000225017.
FT DOMAIN 126 282 ELMO.
SQ SEQUENCE 293 AA; 34961 MW; 339CD216FC46ADD2 CRC64;
MFISLWEFFY GHFFRFWMKW LLRQMTGKCE LQRIFDTYVG AQRTHRIENS LTYSKNKVLQ
KATHVVQSEV DKYVDDIMKE KNINPEKDAS FKICMKMCLL QITGYKQLYL DVESVRKRPY
DSDNLQHEEL LMKLWNLLMP TKKLNARISK QWAEIGFQGD DPKTDFRGMG ILGLINLVYF
SENYTSEAHQ ILSRSNHPKL GYSYAIVGIN LTEMAYSLLK SEALKFHLYN LVPGIPTMEH
FHQFYCYLVY EFDKFWFEEE PESIMYFNLY REKFHEKIKG LLLDCNVALT LKV
//
MIM
610196
*RECORD*
*FIELD* NO
610196
*FIELD* TI
*610196 ELMO/CED12 DOMAIN-CONTAINING PROTEIN 2; ELMOD2
*FIELD* TX
DESCRIPTION
ELMOD2 functions as a GTPase-activating protein (GAP) for members of the
read moreARL (see ARL2, 601175) and ARF (see ARF1, 103180) families of small
GTPases (Bowzard et al., 2007).
CLONING
Strausberg et al. (2002) identified the ELMOD2 gene, which encodes a
293-amino acid protein.
Using RT-PCR Hodgson et al. (2006) found that ELMOD2 mRNA was expressed
in all human tissues and cell types studied, except skeletal muscle.
Using in situ hybridization, the authors recognized expression in
alveolar macrophages and alveolar walls in healthy lung.
By database analysis to identify proteins similar to bovine testis
Elmod2, followed by RT-PCR of a fetal brain cDNA library, Bowzard et al.
(2007) cloned human ELMOD2. The deduced 293-amino acid protein shares
94% identity with bovine Elmod2. ELMOD2 contains a C-terminal ELMO
domain, but it lacks the C-terminal pleckstrin (PLEK; 173570) homology
domain found in larger ELMO domain-containing proteins, such as ELMO1
(606420). Northern blot analysis detected weak expression of a 1.3-kb
transcript in stomach and testis, but not in other human tissues.
Database analysis revealed orthologs of ELMOD2 in vertebrates, but not
in early eukaryotes.
GENE STRUCTURE
The ELMOD2 gene consists of 9 exons (Strausberg et al., 2002).
MAPPING
By genomic sequence analysis, Hodgson et al. (2006) mapped the ELMOD2
gene to chromosome 4q31.
GENE FUNCTION
Bowzard et al. (2007) found that HeLa cells transfected with ELMOD2
showed elevated GAP activity against ARL2, ARL3 (604695), ARF1, and ARF6
(600464), but not RHOA (165390) RAC1, (602048), and RAN (601179). The
GAP activity of recombinant human ELMOD2 or purified bovine Elmod2 was
much less stable than that of the unpurified bovine testis GAP that was
attributed to Elmod2. In the unpurified form, the GAP activity was
associated with a protein complex with an apparent molecular mass of
over 1.3 million Da.
MOLECULAR GENETICS
Hodgson et al. (2006) identified the ELMOD2 gene as a candidate for the
site of the mutation causing familial idiopathic pulmonary fibrosis
(IPF; 178500) in a clustering of cases in the Savo Province of
southeastern Finland. An initial genomewide scan identified 5 loci of
interest. Hierarchical fine mapping in an extended dataset with 24
families originating from the same geographic region revealed a shared
110-kb to 13-Mb haplotype on chromosome 4q31 that was significantly more
frequent among patients than in population-based controls (odds ratio
6.3; 95% CI 2.5-15.9; P = 0.0001). The shared haplotype harbored the
ELMOD2 and LOC152586 (610310) genes. While ELMOD2 expression was
detected in healthy human lung, no specific signal for ELMOD2 was found
in IPF lung samples under several hybridization conditions. Exons 1
through 3 of ELMOD2 were found to be located within the susceptibility
haplotype. All 9 exons and exon-intron boundaries of ELMOD2 were
sequenced in 1 affected patient from each IPF family in which the genome
scan was performed. No mutations were found in the coding regions or
exon-intron boundaries.
*FIELD* RF
1. Bowzard, J. B.; Cheng, D.; Peng, J.; Kahn, R. A.: ELMOD2 is an
Arl2 GTPase-activating protein that also acts on Arfs. J. Biol. Chem. 282:
17568-17580, 2007.
2. Hodgson, U.; Pulkkinen, V.; Dixon, M.; Peyrard-Janvid, M.; Rehn,
M.; Lahermo, P.; Ollikainen, V.; Salmenkivi, K.; Kinnula, V.; Kere,
J.; Tukiainen, P.; Laitinen, T.: ELMOD2 is a candidate gene for familial
idiopathic pulmonary fibrosis. Am. J. Hum. Genet. 79: 149-154, 2006.
3. Strausberg, R. L.; Feingold, E. A.; Grouse, L. H.; Derge, J. G.;
Klausner, R. D.; Collins, F. S.; Wagner, L.; Shenmen, C. M.; Schuler,
G. D.; Altschul, S. F.; Zeeberg, B.; Buetow, K. H.; and 71 others
: Generation and initial analysis of more than 15,000 full-length
human and mouse cDNA sequences. Proc. Nat. Acad. Sci. 99: 16899-16903,
2002.
*FIELD* CN
Patricia A. Hartz - updated: 10/2/2013
*FIELD* CD
Victor A. McKusick: 6/16/2006
*FIELD* ED
mgross: 10/23/2013
tpirozzi: 10/2/2013
mgross: 9/24/2013
wwang: 8/10/2006
alopez: 6/16/2006
*RECORD*
*FIELD* NO
610196
*FIELD* TI
*610196 ELMO/CED12 DOMAIN-CONTAINING PROTEIN 2; ELMOD2
*FIELD* TX
DESCRIPTION
ELMOD2 functions as a GTPase-activating protein (GAP) for members of the
read moreARL (see ARL2, 601175) and ARF (see ARF1, 103180) families of small
GTPases (Bowzard et al., 2007).
CLONING
Strausberg et al. (2002) identified the ELMOD2 gene, which encodes a
293-amino acid protein.
Using RT-PCR Hodgson et al. (2006) found that ELMOD2 mRNA was expressed
in all human tissues and cell types studied, except skeletal muscle.
Using in situ hybridization, the authors recognized expression in
alveolar macrophages and alveolar walls in healthy lung.
By database analysis to identify proteins similar to bovine testis
Elmod2, followed by RT-PCR of a fetal brain cDNA library, Bowzard et al.
(2007) cloned human ELMOD2. The deduced 293-amino acid protein shares
94% identity with bovine Elmod2. ELMOD2 contains a C-terminal ELMO
domain, but it lacks the C-terminal pleckstrin (PLEK; 173570) homology
domain found in larger ELMO domain-containing proteins, such as ELMO1
(606420). Northern blot analysis detected weak expression of a 1.3-kb
transcript in stomach and testis, but not in other human tissues.
Database analysis revealed orthologs of ELMOD2 in vertebrates, but not
in early eukaryotes.
GENE STRUCTURE
The ELMOD2 gene consists of 9 exons (Strausberg et al., 2002).
MAPPING
By genomic sequence analysis, Hodgson et al. (2006) mapped the ELMOD2
gene to chromosome 4q31.
GENE FUNCTION
Bowzard et al. (2007) found that HeLa cells transfected with ELMOD2
showed elevated GAP activity against ARL2, ARL3 (604695), ARF1, and ARF6
(600464), but not RHOA (165390) RAC1, (602048), and RAN (601179). The
GAP activity of recombinant human ELMOD2 or purified bovine Elmod2 was
much less stable than that of the unpurified bovine testis GAP that was
attributed to Elmod2. In the unpurified form, the GAP activity was
associated with a protein complex with an apparent molecular mass of
over 1.3 million Da.
MOLECULAR GENETICS
Hodgson et al. (2006) identified the ELMOD2 gene as a candidate for the
site of the mutation causing familial idiopathic pulmonary fibrosis
(IPF; 178500) in a clustering of cases in the Savo Province of
southeastern Finland. An initial genomewide scan identified 5 loci of
interest. Hierarchical fine mapping in an extended dataset with 24
families originating from the same geographic region revealed a shared
110-kb to 13-Mb haplotype on chromosome 4q31 that was significantly more
frequent among patients than in population-based controls (odds ratio
6.3; 95% CI 2.5-15.9; P = 0.0001). The shared haplotype harbored the
ELMOD2 and LOC152586 (610310) genes. While ELMOD2 expression was
detected in healthy human lung, no specific signal for ELMOD2 was found
in IPF lung samples under several hybridization conditions. Exons 1
through 3 of ELMOD2 were found to be located within the susceptibility
haplotype. All 9 exons and exon-intron boundaries of ELMOD2 were
sequenced in 1 affected patient from each IPF family in which the genome
scan was performed. No mutations were found in the coding regions or
exon-intron boundaries.
*FIELD* RF
1. Bowzard, J. B.; Cheng, D.; Peng, J.; Kahn, R. A.: ELMOD2 is an
Arl2 GTPase-activating protein that also acts on Arfs. J. Biol. Chem. 282:
17568-17580, 2007.
2. Hodgson, U.; Pulkkinen, V.; Dixon, M.; Peyrard-Janvid, M.; Rehn,
M.; Lahermo, P.; Ollikainen, V.; Salmenkivi, K.; Kinnula, V.; Kere,
J.; Tukiainen, P.; Laitinen, T.: ELMOD2 is a candidate gene for familial
idiopathic pulmonary fibrosis. Am. J. Hum. Genet. 79: 149-154, 2006.
3. Strausberg, R. L.; Feingold, E. A.; Grouse, L. H.; Derge, J. G.;
Klausner, R. D.; Collins, F. S.; Wagner, L.; Shenmen, C. M.; Schuler,
G. D.; Altschul, S. F.; Zeeberg, B.; Buetow, K. H.; and 71 others
: Generation and initial analysis of more than 15,000 full-length
human and mouse cDNA sequences. Proc. Nat. Acad. Sci. 99: 16899-16903,
2002.
*FIELD* CN
Patricia A. Hartz - updated: 10/2/2013
*FIELD* CD
Victor A. McKusick: 6/16/2006
*FIELD* ED
mgross: 10/23/2013
tpirozzi: 10/2/2013
mgross: 9/24/2013
wwang: 8/10/2006
alopez: 6/16/2006