ID A0A2U3Y2H0_LEPWE Unreviewed; 299 AA.
AC A0A2U3Y2H0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Prohibitin {ECO:0000256|RuleBase:RU366048};
GN Name=PHB2 {ECO:0000313|RefSeq:XP_006737927.1};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006737927.1};
RN [1] {ECO:0000313|RefSeq:XP_006737927.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006737927.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_006737927.1; XM_006737864.2.
DR AlphaFoldDB; A0A2U3Y2H0; -.
DR STRING; 9713.A0A2U3Y2H0; -.
DR GeneID; 102735974; -.
DR KEGG; lww:102735974; -.
DR CTD; 11331; -.
DR OrthoDB; 1330394at2759; -.
DR Proteomes; UP000245341; Unplaced.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000245341}.
FT DOMAIN 39..201
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
FT COILED 200..238
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 299 AA; 33315 MW; EB35918D7DA0CB75 CRC64;
MAQNLKDLAG RLPSGPRGMG TALKLLLGAG AVAYGVRESV FTVEGGHRAI FFNRIGGVQQ
DTILAEGLHF RIPWFQYPII YDIRARPRKI SSPTGSKDLQ MVNISLRVLS RPNAMELPSM
YQRLGLDYEE RVLPSIVNEV LKSVVAKFNA SQLITQRAQV SLLIRRELTE RAKDFSLILD
DVAITELSFS REYTAAVEAK QVAQQEAQRA QFLVEKAKQE QRQKIVQAEG EAEAAKMLGE
ALSKNPGYIK LRKIRAAQNI SKTIATSQNR IYLTADNLVL NLQDESFTRG SDSLIKGKK
//
