ATLA1_BOVIN
ID ATLA1_BOVIN Reviewed; 558 AA.
AC Q58D72; Q3ZBC1;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Atlastin-1;
DE EC=3.6.5.-;
GN Name=ATL1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: GTPase tethering membranes through formation of trans-
CC homooligomers and mediating homotypic fusion of endoplasmic reticulum
CC membranes. Functions in endoplasmic reticulum tubular network
CC biogenesis. May also regulate Golgi biogenesis. May regulate axonal
CC development. {ECO:0000250|UniProtKB:Q8WXF7}.
CC -!- SUBUNIT: Monomer as apoprotein and in the GDP-bound form. Homodimer in
CC the GTP-bound form. Interacts (via N-terminal region) with MAP4K4 (via
CC CNH regulatory domain). Interacts with REEP5, RTN3 and RTN4 (via the
CC transmembrane region). Interacts with SPAST; interaction is direct.
CC Interacts with REEP1. Interacts with CPT1C. Interacts with ARL6IP1.
CC Interacts with ZFYVE27. {ECO:0000250|UniProtKB:Q6PST4,
CC ECO:0000250|UniProtKB:Q8BH66, ECO:0000250|UniProtKB:Q8WXF7}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8WXF7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8WXF7}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8WXF7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8WXF7}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q6PST4}. Note=Localizes to endoplasmic reticulum
CC tubular network. {ECO:0000250|UniProtKB:Q8BH66}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. GB1/RHD3 GTPase family. GB1 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01052}.
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DR EMBL; BT021725; AAX46572.1; -; mRNA.
DR EMBL; BC103448; AAI03449.1; -; mRNA.
DR RefSeq; NP_001029803.1; NM_001034631.2.
DR RefSeq; XP_005211757.1; XM_005211700.3.
DR AlphaFoldDB; Q58D72; -.
DR SMR; Q58D72; -.
DR STRING; 9913.ENSBTAP00000019032; -.
DR PaxDb; Q58D72; -.
DR PRIDE; Q58D72; -.
DR Ensembl; ENSBTAT00000019032; ENSBTAP00000019032; ENSBTAG00000014312.
DR GeneID; 535424; -.
DR KEGG; bta:535424; -.
DR CTD; 51062; -.
DR VEuPathDB; HostDB:ENSBTAG00000014312; -.
DR VGNC; VGNC:26265; ATL1.
DR eggNOG; KOG2037; Eukaryota.
DR GeneTree; ENSGT00940000158704; -.
DR HOGENOM; CLU_021447_2_0_1; -.
DR InParanoid; Q58D72; -.
DR OMA; GFIHNIW; -.
DR OrthoDB; 1027269at2759; -.
DR TreeFam; TF105251; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000014312; Expressed in occipital lobe and 78 other tissues.
DR ExpressionAtlas; Q58D72; baseline.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; ISS:UniProtKB.
DR GO; GO:0098826; C:endoplasmic reticulum tubular network membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000137; C:Golgi cis cisterna; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISS:UniProtKB.
DR GO; GO:1990809; P:endoplasmic reticulum tubular network membrane organization; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030386; G_GB1_RHD3_dom.
DR InterPro; IPR036543; Guanylate-bd_C_sf.
DR InterPro; IPR015894; Guanylate-bd_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02263; GBP; 1.
DR SUPFAM; SSF48340; SSF48340; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51715; G_GB1_RHD3; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell projection; Coiled coil; Endoplasmic reticulum;
KW Golgi apparatus; GTP-binding; Hydrolase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..558
FT /note="Atlastin-1"
FT /id="PRO_0000238933"
FT TOPO_DOM 1..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 493..558
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 64..309
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..558
FT /note="Sufficient for membrane association"
FT /evidence="ECO:0000250"
FT COILED 418..439
FT /evidence="ECO:0000255"
FT BINDING 74..81
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 118..120
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 217..218
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 276..279
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BH66"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BH66"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BH66"
FT MOD_RES 395
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6DD88"
FT CONFLICT 4..6
FT /note="NRR -> SRK (in Ref. 1; AAX46572)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="T -> G (in Ref. 1; AAX46572)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="P -> S (in Ref. 1; AAX46572)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="V -> I (in Ref. 1; AAX46572)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="H -> Y (in Ref. 1; AAX46572)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="I -> V (in Ref. 1; AAX46572)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="S -> A (in Ref. 1; AAX46572)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="D -> E (in Ref. 1; AAX46572)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="A -> S (in Ref. 1; AAX46572)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="S -> I (in Ref. 1; AAX46572)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="T -> S (in Ref. 1; AAX46572)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="M -> I (in Ref. 1; AAX46572)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 558 AA; 63534 MW; 7ACCBBF0E0C1C577 CRC64;
MAKNRRDRNS WGGFSEKTYE WSSEEEEPVK KAGPVQVLVV KDDHSFELDE TALNRILLSE
AVRDKEVVAV SVAGAFRKGK SFLMDFMLRY MYNQESVDWV GDHNEPLTGF SWRGGSERET
TGIQIWSEIF LINKPDGKKV AVLLMDTQGT FDSQSTLRDS ATVFALSTMI SSIQVYNLSQ
NVQEDDLQHL QLFTEYGRLA MEETFLKPFQ SLIFLVRDWS FPYEFSYGSD GGSKFLEKRL
KVSGNQHEEL QNVRKHIHSC FTKISCFLLP HPGLKVATNP NFDGKLKEID DEFIKNLKIL
IPWLLSPESL DIKEINGNKI TCRGLVEYFK AYIKIYQGEE LPHPKSMLQA TAEANNLAAV
ATAKDTYNKK MEEICGGDKP FLAPNDLQTK HLELKEESVK LFRGVKKMGG EEFSRRYLQQ
LETEIDELYI QYIKHNDSKN IFHAARTPAT LFVVIFITYV IAGVTGFIGL DIIASLCNMI
MGLTLITLCT WAYIRYSGEY RELGAVIDQV AAALWDQGST NEALYKLYSA AATHRHLYHQ
AFPAPKSEST EQSEKKKM
