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PIOS1_RAT
ID   PIOS1_RAT               Reviewed;          54 AA.
AC   C0HLN0;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2020, sequence version 1.
DT   03-AUG-2022, entry version 8.
DE   RecName: Full=Protein PIGBOS1 {ECO:0000305};
DE   AltName: Full=PIGB opposite strand protein 1 homolog {ECO:0000312|RGD:6502569};
GN   Name=Pigbos1 {ECO:0000312|RGD:6502569};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000305}
RP   HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=31653868; DOI=10.1038/s41467-019-12816-z;
RA   Chu Q., Martinez T.F., Novak S.W., Donaldson C.J., Tan D., Vaughan J.M.,
RA   Chang T., Diedrich J.K., Andrade L., Kim A., Zhang T., Manor U.,
RA   Saghatelian A.;
RT   "Regulation of the ER stress response by a mitochondrial microprotein.";
RL   Nat. Commun. 10:4883-4883(2019).
CC   -!- FUNCTION: Plays a role in regulation of the unfolded protein response
CC       triggered by endoplasmic reticulum (ER) stress resulting from the
CC       presence of unfolded proteins in the ER lumen.
CC       {ECO:0000250|UniProtKB:A0A0B4J2F0}.
CC   -!- SUBUNIT: Homooligomer (PubMed:31653868). Interacts (via C-terminus)
CC       with endoplasmic reticulum (ER) protein CLCC1; the interaction occurs
CC       at the mitochondria-associated ER membrane, a zone of contact between
CC       the ER and mitochondrial membranes, but does not appear to play a role
CC       in ER-mitochondria tethering and is not affected by ER stress (By
CC       similarity). {ECO:0000250|UniProtKB:A0A0B4J2F0,
CC       ECO:0000269|PubMed:31653868}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000269|PubMed:31653868}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Detected in a number of tested tissues including
CC       pancreas, brain, heart, kidney, liver, thymus and white adipose tissue
CC       (at protein level). {ECO:0000269|PubMed:31653868}.
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DR   EMBL; AC142458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001295361.1; NM_001308432.1.
DR   AlphaFoldDB; C0HLN0; -.
DR   SMR; C0HLN0; -.
DR   IntAct; C0HLN0; 1.
DR   Ensembl; ENSRNOT00000108954; ENSRNOP00000094136; ENSRNOG00000067122.
DR   GeneID; 100909598; -.
DR   KEGG; rno:100909598; -.
DR   CTD; 101928527; -.
DR   RGD; 6502569; Pigbos1.
DR   GeneTree; ENSGT00760000120436; -.
DR   PRO; PR:C0HLN0; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:UniProtKB.
DR   GO; GO:1900101; P:regulation of endoplasmic reticulum unfolded protein response; ISS:UniProtKB.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Unfolded protein response.
FT   CHAIN           1..54
FT                   /note="Protein PIGBOS1"
FT                   /id="PRO_0000448885"
FT   TOPO_DOM        1..9
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        10..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..54
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          30..36
FT                   /note="Required for interaction with CLCC1"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4J2F0"
SQ   SEQUENCE   54 AA;  6358 MW;  BEE6CA6ABD3CB40C CRC64;
     MLRRLTRPQL LFAAALGVAG GMYIYQPIFE QYSRDQKELK EKVKILQESE EKRS
 
 
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