ID A0A401U427_CHIPU Unreviewed; 121 AA.
AC A0A401U427;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 22-FEB-2023, entry version 11.
DE RecName: Full=SURF1-like protein {ECO:0000256|RuleBase:RU363076};
DE Flags: Fragment;
GN ORFNames=chiPu_0033869 {ECO:0000313|EMBL:GCC49606.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC49606.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC49606.1, ECO:0000313|Proteomes:UP000287033}
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: Probably involved in the biogenesis of the COX complex.
CC {ECO:0000256|RuleBase:RU363076}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|RuleBase:RU363076}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU363076}.
CC -!- SIMILARITY: Belongs to the SURF1 family.
CC {ECO:0000256|RuleBase:RU363076}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU363076}.
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:GCC49606.1}.
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DR EMBL; BEZZ01274265; GCC49606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401U427; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR002994; Surf1/Shy1.
DR Pfam; PF02104; SURF1; 1.
DR PROSITE; PS50895; SURF1; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|RuleBase:RU363076};
KW Mitochondrion {ECO:0000256|RuleBase:RU363076};
KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU363076};
KW Reference proteome {ECO:0000313|Proteomes:UP000287033};
KW Transmembrane {ECO:0000256|RuleBase:RU363076};
KW Transmembrane helix {ECO:0000256|RuleBase:RU363076}.
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363076"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 121
FT /evidence="ECO:0000313|EMBL:GCC49606.1"
SQ SEQUENCE 121 AA; 13066 MW; 165CB205C5B93D27 CRC64;
MAAVDRGDHD PAAAFDEGAA DRAAIPPQGR RRPTDRARPE MNDVSTRRPS AAGFGLFTLI
LIAVFIALGV WQLQRRVEKH ALIAALDARL AAPTEALPPP SAWPTLTSAK DEFRRVTLTA
T
//
