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Database: UniProt
Entry: A0A093REX0_PHACA
LinkDB: A0A093REX0_PHACA
Original site: A0A093REX0_PHACA 
ID   A0A093REX0_PHACA        Unreviewed;       227 AA.
AC   A0A093REX0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Prohibitin {ECO:0000256|RuleBase:RU366048};
DE   Flags: Fragment;
GN   ORFNames=N336_07212 {ECO:0000313|EMBL:KFW94562.1};
OS   Phalacrocorax carbo (Great cormorant) (Pelecanus carbo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Suliformes; Phalacrocoracidae;
OC   Phalacrocorax.
OX   NCBI_TaxID=9209 {ECO:0000313|EMBL:KFW94562.1, ECO:0000313|Proteomes:UP000053238};
RN   [1] {ECO:0000313|EMBL:KFW94562.1, ECO:0000313|Proteomes:UP000053238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N336 {ECO:0000313|EMBL:KFW94562.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protein with pleiotropic attributes mediated in a cell-
CC       compartment- and tissue-specific manner, which include the plasma
CC       membrane-associated cell signaling functions, mitochondrial chaperone,
CC       and transcriptional co-regulator of transcription factors and sex
CC       steroid hormones in the nucleus. {ECO:0000256|ARBA:ARBA00037479}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|ARBA:ARBA00004273, ECO:0000256|RuleBase:RU366048}.
CC   -!- SIMILARITY: Belongs to the prohibitin family.
CC       {ECO:0000256|ARBA:ARBA00009658, ECO:0000256|RuleBase:RU366048}.
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DR   EMBL; KL442498; KFW94562.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093REX0; -.
DR   Proteomes; UP000053238; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd03401; SPFH_prohibitin; 1.
DR   Gene3D; 3.30.479.30; Band 7 domain; 1.
DR   InterPro; IPR001107; Band_7.
DR   InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR   InterPro; IPR000163; Prohibitin.
DR   PANTHER; PTHR23222; PROHIBITIN; 1.
DR   PANTHER; PTHR23222:SF1; PROHIBITIN-2; 1.
DR   Pfam; PF01145; Band_7; 1.
DR   PRINTS; PR00679; PROHIBITIN.
DR   SMART; SM00244; PHB; 1.
DR   SUPFAM; SSF117892; Band 7/SPFH domain; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00022792, ECO:0000256|RuleBase:RU366048};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW   ECO:0000256|RuleBase:RU366048};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053238}.
FT   DOMAIN          1..131
FT                   /note="Band 7"
FT                   /evidence="ECO:0000259|SMART:SM00244"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFW94562.1"
FT   NON_TER         227
FT                   /evidence="ECO:0000313|EMBL:KFW94562.1"
SQ   SEQUENCE   227 AA;  25863 MW;  4898F410504EED94 CRC64;
     RIPWFQYPII YDIRARPRKI SSPTGSKDLQ MVNISLRVLT RPNAAELPSM YQRLGLDYEE
     RVLPSIVNEV LKSVVAKFNA SQLITQRAQV SLLIRRELTE RAKDFSLILD DVAITELSFS
     REYTAAVEAK QVAQQEAQRA QFLVEKAKQE QKQKIVQAEG EATAAKMISC LGKFCVMWLV
     SLTVLRICHS GLTLRRLLSD DSFNSQNRVY LTADNLVLNL QDEGFTR
//
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