ID A0A1S3T407_SALSA Unreviewed; 1061 AA.
AC A0A1S3T407;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Dynamin-like 120 kDa protein, mitochondrial {ECO:0000256|ARBA:ARBA00018307};
DE EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
GN Name=LOC106613511 {ECO:0000313|RefSeq:XP_014071323.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014071323.1};
RN [1] {ECO:0000313|RefSeq:XP_014071323.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014071323.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001837};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004434}. Mitochondrion membrane
CC {ECO:0000256|ARBA:ARBA00004325}.
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DR RefSeq; XP_014071323.1; XM_014215848.1.
DR AlphaFoldDB; A0A1S3T407; -.
DR GeneID; 106613511; -.
DR KEGG; sasa:106613511; -.
DR OrthoDB; 48011at2759; -.
DR Proteomes; UP000087266; Chromosome ssa10.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR022812; Dynamin.
DR InterPro; IPR001401; Dynamin_GTPase.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR045817; OPA1_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11566; DYNAMIN; 1.
DR PANTHER; PTHR11566:SF67; DYNAMIN-LIKE 120 KDA PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF19434; OPA1_C; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
PE 4: Predicted;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 386..662
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT REGION 254..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..302
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1061 AA; 121740 MW; E823DDDC0B8C2505 CRC64;
MLRVGRAVAC MACKNMVSNN MGVRFRMPLQ KLHPLSRAIH HRYNASANPQ RPPHCSAARH
FTSMSRLPMR PPKPPPGGHG GWRYQQHRNF WMLRLASRLL KLRYIVLGSA VGGGYTAKKT
YEEWKDMLPD MSAYNWVIPD FVWELSDQID LDKLTKILPE LEEIAKLLPE LPDFDKIGEN
FTFLKSILST GVSVGSEGAS GLRLLLAEAP GDTPVKAATE APVTATPEAS DKQFKKGLLG
ELILIQQQIQ QAEEEVRRAA ASKNARPSPE PAPSPPPRPP PPPRLIPEPM PTTTPNPSPS
PPQQKRKSSD KEKVDQLQEE LLRTQMKYQR MLERLEKENK DLRKVVLQKD EKGIHQRKIK
VCKSLIDMYS EVLDILSDFD SNYNTQDHLP RVVVVGDQSA GKTSVLEMIA QARIFPRGSG
EMMTRSPVKV TLSEGPHHVA MFKDSSREFD LGKEEDLAAL RHEIELRMRK SVKEGQTVSP
ETISLSVKGP GIQRMVLVDL PGVISTVTAG MAADTKETIF SISKNYMQNP NAIILCIQDG
SVDAERSIVT DLVSQMDPQG KRTIFVLTKV DLAEKNLASP NRIQQIVEGK LFPMKALGYF
AVVTGKGSAG ESIDSIKDYE EDFFQNSRLL RDGMLKAHQV TTKNLSLAVS DCFWKMVRES
VEQQADAFKA SRFNLETEWK NNYPRLRELD RNELFEKAKN EILDEVISLS QVTPKHWEAI
LQKKLWERVS THVIENIYLP AAQTMNSGTF NTTVDIKLKQ WTDKQLPHKA LEVAWETLQE
EFARFMAEYK GKDQDDIFDK LKEAVKDESI KRHKWNERAM DSLRVIQHNA LEDRSITDKP
QWDAAIQFME ETLQARLKDT DSVINDMVGP DWKQRWMSWK NRSPEQHTRN ETRNELERLL
KLHEDHTAYL ANDEVTTVRK NLEGRGVEVD PALIKDTWHQ LYRRHFLQKA LQHCNLCRRG
FYYYQRHFVD SELECNDVVL FWRIQRMLLI TANTLRQQLT NTEVRRLEKN VKEVLEDFGE
DNEKKVHLIT GRRVQLAEDL KKVREIQEKL EAFIEALHKE K
//
