ID A0A401PKJ6_SCYTO Unreviewed; 981 AA.
AC A0A401PKJ6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Mitochondrial fission regulator {ECO:0000256|RuleBase:RU369053};
DE Flags: Fragment;
GN ORFNames=scyTo_0002688 {ECO:0000313|EMBL:GCB73608.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB73608.1, ECO:0000313|Proteomes:UP000288216};
RN [1] {ECO:0000313|EMBL:GCB73608.1, ECO:0000313|Proteomes:UP000288216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
CC -!- FUNCTION: Plays a role in mitochondrial aerobic respiration. Regulates
CC mitochondrial organization and fission.
CC {ECO:0000256|RuleBase:RU369053}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU369053}.
CC -!- SIMILARITY: Belongs to the MTFR1 family.
CC {ECO:0000256|ARBA:ARBA00005807, ECO:0000256|RuleBase:RU369053}.
CC -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC subfamily. {ECO:0000256|ARBA:ARBA00008214}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCB73608.1}.
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DR EMBL; BFAA01000688; GCB73608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401PKJ6; -.
DR STRING; 75743.A0A401PKJ6; -.
DR OMA; VTKMSIF; -.
DR Proteomes; UP000288216; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0009060; P:aerobic respiration; IEA:UniProtKB-UniRule.
DR GO; GO:0000266; P:mitochondrial fission; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.58.630; -; 1.
DR Gene3D; 6.10.30.30; -; 1.
DR Gene3D; 1.10.20.40; Formin, diaphanous GTPase-binding domain; 1.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR Gene3D; 1.10.238.150; Formin, FH3 diaphanous domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014767; DAD_dom.
DR InterPro; IPR044933; DIA_GBD_sf.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR InterPro; IPR007972; Mtfr1.
DR PANTHER; PTHR45691; PROTEIN DIAPHANOUS; 1.
DR PANTHER; PTHR45691:SF9; PROTEIN DIAPHANOUS HOMOLOG 3; 1.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR Pfam; PF05308; Mito_fiss_reg; 1.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51231; DAD; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Mitochondrion {ECO:0000256|RuleBase:RU369053};
KW Reference proteome {ECO:0000313|Proteomes:UP000288216}.
FT DOMAIN 1..359
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 517..914
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 937..967
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 449..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 399..433
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 463..499
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..938
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:GCB73608.1"
SQ SEQUENCE 981 AA; 113887 MW; 24ACF649C665E9D9 CRC64;
FSDLLRLCWT MEDMNLNEER KAPLRKKDLS IKREMVVQYI GGTSNTGSLK NRQFTAILPH
EFIQELKSGV ADERLLSSLE SLRVSLSSNP ISWVGSFGHE GLNQLLDILE KLLNKKHQEK
NDRKCQHKVI QCLRAFMNNK YGLERILGEE RSIFLLARAI DPKQPNMMTD AIKLLSAICI
VGEENILENV LEAITTAGEL RKWERFYPIV EGLHDTPVQL KVACMQFINA LVTTPDDLDL
RMHIRNEFVR CGLREILLEL RLIKNDALDI QLKVFDEHKE EDLIEFSHRL EDIRSELDEM
NDVYNMLFNT VKDTRAESYF LSILQHLLLI RNDYFVRPQY FKIIEECVSQ IVLHRSGMDP
DFTYRKRLDV NFDHLVDICV DKARSDECEQ RLSELTRKFD EEFTTRQEAQ AQMQKKEEKI
NELEAELQNL KVQLSALPPD VRATVTGAQN KARHNNSLSS TLHGGPPPPP PSLISGSLPP
PPPPPPPPPP PPPPPATGFK EGHWSPTPQT LPHGLKPKKK FKLDINMKRV NWCKIRPLEM
PENCFWIKAN DDKYENPDLF ARISFIFGAQ KRGKKDEEYE EKKDIKKRIK ELKVLDPKTA
QNLSIFLGSF RMPYEEIKTI ILEVDEEQLT ESIIQNLVSH LPEQEQVLTL ARFKNDYNSL
SEPEQFGVVM SSIKKLRPRL NAILFKLQFE EQVNNIRPDI MTVTTACEEL KKSKRFGNLL
ELVLLIGNYM NAGSRNAQTY GFNINFLCKL NDTKSADQKV TFLHFLTQVC EEKYPDILKF
TDDLQHVDKA SKVCAENLEK NLKQMEKQLQ QLEKDLETFP PPEDRHDKFV TKMSRFASHA
REDYHKLANM HRSMEKLYHE LMHYFVINPK KVTAEELFSD ISNFRSMFMQ AMKENVKRRE
ATEKLRLAKL AKEKVEKEKR ERQQKKRHLL EKNSEGDETG VMDSLLEALQ SGAAFRDRRK
RTPRPKGLVN TLVYKSAKEK S
//
