RBCC

Full text data of ATL3

ATL3 [Confidence: high (present in two of the MS resources)]
Atlastin-3; 3.6.5.-

hRBCD IPI00383828
IPI00383828 Hypothetical protein DKFZp564J0863 Hypothetical protein DKFZp564J0863 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 2 n/a n/a n/a n/a 3 2 not mentioned n/a found at its expected molecular weight found at molecular weight

UniProt Q6DD88
ID ATLA3_HUMAN Reviewed; 541 AA.
AC Q6DD88; Q8N7W5; Q9H8Q5; Q9UFL1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2004, sequence version 1.
DT 22-JAN-2014, entry version 79.
DE RecName: Full=Atlastin-3;
DE EC=3.6.5.-;
GN Name=ATL3;
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=Ovary, and 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 MRNA].
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
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 IDENTIFICATION.
RX PubMed=14506257; DOI=10.1074/jbc.M306702200;
RA Zhu P.-P., Patterson A., Lavoie B., Stadler J., Shoeb M., Patel R.,
RA Blackstone C.;
RT "Cellular localization, oligomerization, and membrane association of
RT the hereditary spastic paraplegia 3A (SPG3A) protein atlastin.";
RL J. Biol. Chem. 278:49063-49071(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [6]
RP FUNCTION, TOPOLOGY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-73 AND
RP ARG-213, AND TISSUE SPECIFICITY.
RX PubMed=18270207; DOI=10.1093/hmg/ddn046;
RA Rismanchi N., Soderblom C., Stadler J., Zhu P.-P., Blackstone C.;
RT "Atlastin GTPases are required for Golgi apparatus and ER
RT morphogenesis.";
RL Hum. Mol. Genet. 17:1591-1604(2008).
RN [7]
RP FUNCTION.
RX PubMed=19665976; DOI=10.1016/j.cell.2009.05.025;
RA Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A.,
RA Rapoport T.A., Blackstone C.;
RT "A class of dynamin-like GTPases involved in the generation of the
RT tubular ER network.";
RL Cell 138:549-561(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-391, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
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: GTPase tethering membranes through formation of trans-
CC homooligomers and mediating homotypic fusion of endoplasmic
CC reticulum membranes. Functions in endoplasmic reticulum tubular
CC network biogenesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in peripheral tissues (at protein
CC level).
CC -!- SIMILARITY: Belongs to the GBP family. Atlastin subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC05111.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing;
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DR EMBL; AK097588; BAC05111.1; ALT_SEQ; mRNA.
DR EMBL; AK023383; BAB14552.1; -; mRNA.
DR EMBL; AL117600; CAB56010.2; -; mRNA.
DR EMBL; BC077727; AAH77727.1; -; mRNA.
DR PIR; T17320; T17320.
DR RefSeq; NP_056274.3; NM_015459.3.
DR UniGene; Hs.356719; -.
DR ProteinModelPortal; Q6DD88; -.
DR SMR; Q6DD88; 23-436.
DR IntAct; Q6DD88; 2.
DR MINT; MINT-3308360; -.
DR PhosphoSite; Q6DD88; -.
DR DMDM; 74736374; -.
DR PaxDb; Q6DD88; -.
DR PeptideAtlas; Q6DD88; -.
DR PRIDE; Q6DD88; -.
DR Ensembl; ENST00000398868; ENSP00000381844; ENSG00000184743.
DR GeneID; 25923; -.
DR KEGG; hsa:25923; -.
DR UCSC; uc001nxk.1; human.
DR CTD; 25923; -.
DR GeneCards; GC11M063391; -.
DR HGNC; HGNC:24526; ATL3.
DR MIM; 609369; gene.
DR neXtProt; NX_Q6DD88; -.
DR PharmGKB; PA164716353; -.
DR eggNOG; NOG325148; -.
DR HOGENOM; HOG000234332; -.
DR HOVERGEN; HBG062891; -.
DR KO; K17339; -.
DR OrthoDB; EOG7H4DTH; -.
DR GenomeRNAi; 25923; -.
DR NextBio; 47447; -.
DR PRO; PR:Q6DD88; -.
DR ArrayExpress; Q6DD88; -.
DR Bgee; Q6DD88; -.
DR CleanEx; HS_ATL3; -.
DR Genevestigator; Q6DD88; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; NAS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR InterPro; IPR003191; Guanylate-bd_C.
DR InterPro; IPR015894; Guanylate-bd_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02263; GBP; 1.
DR Pfam; PF02841; GBP_C; 1.
DR SUPFAM; SSF48340; SSF48340; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Complete proteome; Endoplasmic reticulum;
KW GTP-binding; Hydrolase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1 541 Atlastin-3.
FT /FTId=PRO_0000287109.
FT TOPO_DOM 1 445 Cytoplasmic.
FT TRANSMEM 446 466 Helical; (Potential).
FT TOPO_DOM 467 467 Lumenal (Potential).
FT TRANSMEM 468 488 Helical; (Potential).
FT TOPO_DOM 489 541 Cytoplasmic.
FT NP_BIND 67 74 GTP (By similarity).
FT NP_BIND 114 116 GTP (By similarity).
FT NP_BIND 213 214 GTP (By similarity).
FT NP_BIND 272 275 GTP (By similarity).
FT MOD_RES 391 391 N6-acetyllysine.
FT MOD_RES 535 535 Phosphoserine.
FT MUTAGEN 73 73 K->A: Alters endoplasmic reticulum
FT morphogenesis.
FT MUTAGEN 213 213 R->Q: Alters endoplasmic reticulum
FT morphogenesis.
FT CONFLICT 49 49 I -> T (in Ref. 1; BAB14552).
FT CONFLICT 158 158 T -> A (in Ref. 2; CAB56010).
FT CONFLICT 173 173 N -> S (in Ref. 1; BAC05111).
FT CONFLICT 202 202 Q -> R (in Ref. 2; CAB56010).
FT CONFLICT 215 215 W -> R (in Ref. 2; CAB56010).
FT CONFLICT 351 351 N -> Y (in Ref. 2; CAB56010).
SQ SEQUENCE 541 AA; 60542 MW; E5C58A53F93B42D0 CRC64;
MLSPQRVAAA ASRGADDAME SSKPGPVQVV LVQKDQHSFE LDEKALASIL LQDHIRDLDV
VVVSVAGAFR KGKSFILDFM LRYLYSQKES GHSNWLGDPE EPLTGFSWRG GSDPETTGIQ
IWSEVFTVEK PGGKKVAVVL MDTQGAFDSQ STVKDCATIF ALSTMTSSVQ IYNLSQNIQE
DDLQQLQLFT EYGRLAMDEI FQKPFQTLMF LVRDWSFPYE YSYGLQGGMA FLDKRLQVKE
HQHEEIQNVR NHIHSCFSDV TCFLLPHPGL QVATSPDFDG KLKDIAGEFK EQLQALIPYV
LNPSKLMEKE INGSKVTCRG LLEYFKAYIK IYQGEDLPHP KSMLQATAEA NNLAAAASAK
DIYYNNMEEV CGGEKPYLSP DILEEKHCEF KQLALDHFKK TKKMGGKDFS FRYQQELEEE
IKELYENFCK HNGSKNVFST FRTPAVLFTG IVALYIASGL TGFIGLEVVA QLFNCMVGLL
LIALLTWGYI RYSGQYRELG GAIDFGAAYV LEQASSHIGN STQATVRDAV VGRPSMDKKA
Q
//

MIM 609369
*RECORD*
*FIELD* NO
609369
*FIELD* TI
*609369 ATLASTIN GTPase 3; ATL3
*FIELD* TX

DESCRIPTION

The ATL3 gene encodes a member of the atlastin family of endoplasmic
read morereticulum-shaping membrane-bound GTPases (summary by Kornak et al.,
2014).

CLONING

By searching databases for sequences similar to atlastin-1 (ATL1;
606439), Zhu et al. (2003) identified atlastin-3. The deduced 567-amino
acid protein contains GTP-binding motifs in its N-terminal half and 2
transmembrane domains in its C-terminal half.

Kornak et al. (2014) stated that ATL3 is expressed in the central
nervous system and in dorsal root ganglia neurons. Expression of the
gene in COS-7 cells showed that it localized to endoplasmic reticulum
tubules and accumulated in punctuate structures corresponding to 3-way
junctions, which represent crossing-points at which the tubules build a
polygonal network.

MAPPING

Zhu et al. (2003) stated that the atlastin-3 gene maps to chromosome
11q13.1.

MOLECULAR GENETICS

In affected members of a 4-generation German family with hereditary
sensory neuropathy type IF (HSN1F; 615632), Kornak et al. (2014)
identified a heterozygous missense mutation in the ATL3 gene (Y192C;
609369.0001). The mutation, which was found by whole-exome sequencing
and confirmed by Sanger sequencing, segregated with the disorder in the
family. Screening of the ATL3 gene in 115 probands with various types of
sensory neuropathy identified the same heterozygous Y192C substitution
in 3 affected members of a Spanish family with a similar phenotype. The
disorder was characterized by sensory neuropathy affecting only the
lower limbs. Distal sensory impairment became apparent during the second
or third decade of life, resulting in painless ulceration of the feet
with poor healing, which progressed to osteomyelitis, bony destruction,
and amputation. In vitro functional expression studies in COS-7 cells
showed that the Y192C mutation caused mislocalization of the protein and
had a dominant-negative disruptive effect on the regular structure of
the endoplasmic reticulum. The findings contributed to the emerging
concept that pathogenic alterations in membrane-shaping proteins
contribute to axonal degeneration.

*FIELD* AV
.0001
NEUROPATHY, HEREDITARY SENSORY, TYPE IF
ATL3, TYR192CYS

In affected members of a 4-generation German family with hereditary
sensory neuropathy type IF (HSN1F; 615632), Kornak et al. (2014)
identified a heterozygous c.575A-G transition in the ATL3 gene,
resulting in a tyr192-to-cys (Y192C) substitution at a highly conserved
residue in the GTPase domain. The mutation, which was found by
whole-exome sequencing and confirmed by Sanger sequencing, segregated
with the disorder in the family. It was not present in the dbSNP, 1000
Genomes Project, or Exome Variant Server databases. Screening of the
ATL3 gene in 115 probands with various types of sensory neuropathy
identified the same heterozygous Y192C substitution in 3 affected
members of a Spanish family with a similar phenotype. Haplotype analysis
suggested a founder effect. In vitro functional expression studies in
COS-7 cells showed that the mutation caused mislocalization of the
protein, i.e., it did not associate normally with 3-way junctions in the
endoplasmic reticulum, but rather accumulated in condensed structures
near the nucleus and localized to unbranched tubules. The mutant protein
had a dominant-negative disruptive effect on the regular structure of
the endoplasmic reticulum.

*FIELD* RF
1. Kornak, U.; Mademan, I.; Schinke, M.; Voigt, M.; Krawitz, P.; Hecht,
J.; Barvencik, F.; Schinke, T.; Giesselmann, S.; Beil, F. T.; Pou-Serradell,
A.; Vilchez, J. J.; and 11 others: Sensory neuropathy with bone
destruction due to a mutation in the membrane-shaping atlastin GTPase
3. Brain 22Jan, 2014. Note: Advance Electronic Publication.

2. Zhu, P.-P.; Patterson, A.; Lavoie, B.; Stadler, J.; Shoeb, M.;
Patel, R.; Blackstone, C.: Cellular localization, oligomerization,
and membrane association of the hereditary spastic paraplegia 3A (SPG3A)
protein atlastin. J. Biol. Chem. 278: 49063-49071, 2003.

*FIELD* CN
Cassandra L. Kniffin - updated: 2/10/2014

*FIELD* CD
Patricia A. Hartz: 5/16/2005

*FIELD* ED
carol: 02/12/2014
mcolton: 2/10/2014
ckniffin: 2/10/2014
mgross: 2/22/2011
wwang: 2/21/2011
mgross: 5/16/2005

RBCC Red Blood Cell Collection

Full text data of ATL3