PIOS1_HUMAN
ID PIOS1_HUMAN Reviewed; 54 AA.
AC A0A0B4J2F0;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Protein PIGBOS1 {ECO:0000305};
DE AltName: Full=PIGB opposite strand protein 1 {ECO:0000312|HGNC:HGNC:50696};
GN Name=PIGBOS1 {ECO:0000312|HGNC:HGNC:50696};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retinoblastoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [3]
RP PROTEIN SEQUENCE OF 43-52, FUNCTION, HOMOOLIGOMERIZATION, INTERACTION WITH
RP CLCC1, SUBCELLULAR LOCATION, CLCC1-INTERACTING REGION, AND MUTAGENESIS OF
RP 30-GLU--TYR-32; 34-LYS--GLN-36; 37-LYS--LEU-39; 40-LYS--LYS-42;
RP 43-MET--LEU-45; 46-VAL--GLU-48; 49-SER--GLU-51 AND 52-LYS--SER-54.
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:0000269|PubMed:31653868}.
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
CC (PubMed:31653868). {ECO:0000269|PubMed:31653868}.
CC -!- INTERACTION:
CC A0A0B4J2F0; Q96S66: CLCC1; NbExp=11; IntAct=EBI-26657479, EBI-2836109;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:31653868}; Single-pass membrane protein
CC {ECO:0000255}.
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DR EMBL; AB593170; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC018926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS81884.1; -.
DR RefSeq; NP_001295350.1; NM_001308421.1.
DR RefSeq; NP_001295351.1; NM_001308422.1.
DR RefSeq; NP_001295352.1; NM_001308423.1.
DR AlphaFoldDB; A0A0B4J2F0; -.
DR SMR; A0A0B4J2F0; -.
DR IntAct; A0A0B4J2F0; 2.
DR BioMuta; PIGBOS1; -.
DR EPD; A0A0B4J2F0; -.
DR jPOST; A0A0B4J2F0; -.
DR MassIVE; A0A0B4J2F0; -.
DR PeptideAtlas; A0A0B4J2F0; -.
DR DNASU; 101928527; -.
DR Ensembl; ENST00000436697.3; ENSP00000484893.1; ENSG00000225973.4.
DR Ensembl; ENST00000567948.1; ENSP00000482636.1; ENSG00000225973.4.
DR GeneID; 101928527; -.
DR KEGG; hsa:101928527; -.
DR MANE-Select; ENST00000436697.3; ENSP00000484893.1; NM_001308421.2; NP_001295350.1.
DR CTD; 101928527; -.
DR GeneCards; PIGBOS1; -.
DR HGNC; HGNC:50696; PIGBOS1.
DR HPA; ENSG00000225973; Low tissue specificity.
DR MalaCards; PIGBOS1; -.
DR MIM; 618809; gene.
DR neXtProt; NX_A0A0B4J2F0; -.
DR VEuPathDB; HostDB:ENSG00000225973; -.
DR eggNOG; ENOG502TEA1; Eukaryota.
DR GeneTree; ENSGT00760000120436; -.
DR HOGENOM; CLU_3049645_0_0_1; -.
DR OMA; GGMYIYQ; -.
DR OrthoDB; 1635233at2759; -.
DR PathwayCommons; A0A0B4J2F0; -.
DR SIGNOR; A0A0B4J2F0; -.
DR BioGRID-ORCS; 101928527; 0 hits in 7 CRISPR screens.
DR ChiTaRS; PIGBOS1; human.
DR Pharos; A0A0B4J2F0; Tdark.
DR PRO; PR:A0A0B4J2F0; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; A0A0B4J2F0; protein.
DR Bgee; ENSG00000225973; Expressed in monocyte and 97 other tissues.
DR ExpressionAtlas; A0A0B4J2F0; baseline and differential.
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; IMP:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Unfolded protein response.
FT CHAIN 1..54
FT /note="Protein PIGBOS1"
FT /id="PRO_0000433799"
FT TOPO_DOM 1..4
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:31653868"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:31653868"
FT REGION 30..36
FT /note="Required for interaction with CLCC1"
FT /evidence="ECO:0000269|PubMed:31653868"
FT MUTAGEN 30..32
FT /note="EQY->AAA: Does not affect mitochondrial location but
FT reduces interaction with CLCC1."
FT /evidence="ECO:0000269|PubMed:31653868"
FT MUTAGEN 34..36
FT /note="KDQ->AAA: Does not affect mitochondrial location but
FT reduces interaction with CLCC1."
FT /evidence="ECO:0000269|PubMed:31653868"
FT MUTAGEN 37..39
FT /note="KEL->AAA: Does not affect mitochondrial location or
FT interaction with CLCC1."
FT /evidence="ECO:0000269|PubMed:31653868"
FT MUTAGEN 40..42
FT /note="KEK->AAA: Does not affect mitochondrial location or
FT interaction with CLCC1."
FT /evidence="ECO:0000269|PubMed:31653868"
FT MUTAGEN 43..45
FT /note="MQL->AAA: Does not affect mitochondrial location or
FT interaction with CLCC1."
FT /evidence="ECO:0000269|PubMed:31653868"
FT MUTAGEN 46..48
FT /note="VQE->AAA: Does not affect mitochondrial location or
FT interaction with CLCC1."
FT /evidence="ECO:0000269|PubMed:31653868"
FT MUTAGEN 49..51
FT /note="SEE->AAA: Does not affect mitochondrial location or
FT interaction with CLCC1."
FT /evidence="ECO:0000269|PubMed:31653868"
FT MUTAGEN 52..54
FT /note="KKS->AAA: Does not affect mitochondrial location or
FT interaction with CLCC1."
FT /evidence="ECO:0000269|PubMed:31653868"
SQ SEQUENCE 54 AA; 6313 MW; 15E9C5F5E988F663 CRC64;
MFRRLTFAQL LFATVLGIAG GVYIFQPVFE QYAKDQKELK EKMQLVQESE EKKS
