PDC6I_RAT
ID PDC6I_RAT Reviewed; 873 AA.
AC Q9QZA2;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Programmed cell death 6-interacting protein;
DE AltName: Full=ALG-2-interacting protein 1;
GN Name=Pdcd6ip; Synonyms=Aip1;
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]
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]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 473-873, AND INTERACTION WITH SH3KBP1.
RX PubMed=10858458; DOI=10.1074/jbc.m908994199;
RA Chen B., Borinstein S.C., Gillis J., Sykes V.W., Bogler O.;
RT "The glioma-associated protein SETA interacts with AIP1/Alix and ALG-2 and
RT modulates apoptosis in astrocytes.";
RL J. Biol. Chem. 275:19275-19281(2000).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=19343716; DOI=10.1002/pmic.200800664;
RA Maurya D.K., Sundaram C.S., Bhargava P.;
RT "Proteome profile of the mature rat olfactory bulb.";
RL Proteomics 9:2593-2599(2009).
CC -!- FUNCTION: Multifunctional protein involved in endocytosis,
CC multivesicular body biogenesis, membrane repair, cytokinesis, apoptosis
CC and maintenance of tight junction integrity. Class E VPS protein
CC involved in concentration and sorting of cargo proteins of the
CC multivesicular body (MVB) for incorporation into intralumenal vesicles
CC (ILVs) that are generated by invagination and scission from the
CC limiting membrane of the endosome. Binds to the phospholipid
CC lysobisphosphatidic acid (LBPA) which is abundant in MVBs internal
CC membranes. The MVB pathway requires the sequential function of ESCRT-O,
CC -I,-II and -III complexes. The ESCRT machinery also functions in
CC topologically equivalent membrane fission events, such as the terminal
CC stages of cytokinesis. Adapter for a subset of ESCRT-III proteins, such
CC as CHMP4, to function at distinct membranes. Required for completion of
CC cytokinesis. May play a role in the regulation of both apoptosis and
CC cell proliferation. Regulates exosome biogenesis in concert with SDC1/4
CC and SDCBP (By similarity). By interacting with F-actin, PARD3 and TJP1
CC secures the proper assembly and positioning of actomyosin-tight
CC junction complex at the apical sides of adjacent epithelial cells that
CC defines a spatial membrane domain essential for the maintenance of
CC epithelial cell polarity and barrier (By similarity).
CC {ECO:0000250|UniProtKB:Q8WUM4, ECO:0000250|UniProtKB:Q9WU78}.
CC -!- SUBUNIT: Self-associates (By similarity). Interacts with SH3KBP1
CC (PubMed:10858458). Interacts with PDCD6 in a calcium-dependent manner
CC (By similarity). Interacts with TSG101 in a calcium-dependent manner;
CC PDCD6IP homooligomerization may be required for TSG101-binding (By
CC similarity). Interacts with SGSM3 (By similarity). Directly interacts
CC with CHMP4A, CHMP4B and CHMP4C (By similarity). Directly interacts with
CC CEP55 in a 1:2 stoechiometry; this interaction is required for PDCD6IP
CC targeting to the midbody (By similarity). May interact with PDGFRB (By
CC similarity). Interacts with SH3GL1 and SH3GL2/endophilin-1 (By
CC similarity). Forms a complex with SDCBP and SDC2 (By similarity). Found
CC in a complex with F-actin, TJP1/ZO-1 and PARD3 (By similarity).
CC Interacts with CD2AP (By similarity). Interacts with ARRDC1 (By
CC similarity). {ECO:0000250|UniProtKB:Q8WUM4,
CC ECO:0000250|UniProtKB:Q9WU78, ECO:0000269|PubMed:10858458}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19343716}.
CC Melanosome {ECO:0000250|UniProtKB:Q8WUM4}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q8WUM4}. Secreted, extracellular exosome
CC {ECO:0000250|UniProtKB:Q8WUM4}. Cell junction, tight junction
CC {ECO:0000250|UniProtKB:Q9WU78}. Midbody, Midbody ring
CC {ECO:0000250|UniProtKB:Q8WUM4}. Note=Colocalized with CEP55 in the
CC midbody during cytokinesis and at centrosomes in non-dividing cells (By
CC similarity). Component of the actomyosin-tight junction complex (By
CC similarity). {ECO:0000250|UniProtKB:Q8WUM4,
CC ECO:0000250|UniProtKB:Q9WU78}.
CC -!- TISSUE SPECIFICITY: Expressed in astrocytes and glioma cells.
CC -!- PTM: May be phosphorylated on tyrosine residues by activated PDGFRB.
CC {ECO:0000250|UniProtKB:Q8WUM4}.
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DR EMBL; AABR03063785; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03064061; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF192757; AAF07179.1; -; mRNA.
DR RefSeq; XP_006244059.1; XM_006243997.2.
DR AlphaFoldDB; Q9QZA2; -.
DR SMR; Q9QZA2; -.
DR BioGRID; 272390; 1.
DR STRING; 10116.ENSRNOP00000012114; -.
DR iPTMnet; Q9QZA2; -.
DR PhosphoSitePlus; Q9QZA2; -.
DR World-2DPAGE; 0004:Q9QZA2; -.
DR jPOST; Q9QZA2; -.
DR PaxDb; Q9QZA2; -.
DR PRIDE; Q9QZA2; -.
DR Ensembl; ENSRNOT00000012114; ENSRNOP00000012114; ENSRNOG00000008981.
DR GeneID; 501083; -.
DR UCSC; RGD:68357; rat.
DR CTD; 10015; -.
DR RGD; 68357; Pdcd6ip.
DR eggNOG; KOG2220; Eukaryota.
DR GeneTree; ENSGT01040000240872; -.
DR HOGENOM; CLU_007181_2_0_1; -.
DR InParanoid; Q9QZA2; -.
DR OrthoDB; 550620at2759; -.
DR PhylomeDB; Q9QZA2; -.
DR Reactome; R-RNO-5213460; RIPK1-mediated regulated necrosis.
DR Reactome; R-RNO-5675482; Regulation of necroptotic cell death.
DR PRO; PR:Q9QZA2; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Genevisible; Q9QZA2; RN.
DR GO; GO:0042641; C:actomyosin; ISS:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISO:RGD.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
DR GO; GO:0090543; C:Flemming body; ISS:UniProtKB.
DR GO; GO:0001772; C:immunological synapse; ISO:RGD.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046983; F:protein dimerization activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0031871; F:proteinase activated receptor binding; ISO:RGD.
DR GO; GO:0017124; F:SH3 domain binding; IDA:RGD.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISS:UniProtKB.
DR GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; ISS:UniProtKB.
DR GO; GO:0061952; P:midbody abscission; ISO:RGD.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IEA:InterPro.
DR GO; GO:1903543; P:positive regulation of exosomal secretion; ISO:RGD.
DR GO; GO:1903553; P:positive regulation of extracellular exosome assembly; ISO:RGD.
DR GO; GO:0051260; P:protein homooligomerization; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0010824; P:regulation of centrosome duplication; ISO:RGD.
DR GO; GO:1903551; P:regulation of extracellular exosome assembly; ISO:RGD.
DR GO; GO:0090559; P:regulation of membrane permeability; ISS:UniProtKB.
DR GO; GO:0090611; P:ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway; ISO:RGD.
DR GO; GO:0046755; P:viral budding; ISO:RGD.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; ISO:RGD.
DR Gene3D; 1.25.40.280; -; 1.
DR InterPro; IPR025304; ALIX_V_dom.
DR InterPro; IPR045251; BRO1-like.
DR InterPro; IPR004328; BRO1_dom.
DR InterPro; IPR038499; BRO1_sf.
DR PANTHER; PTHR23030; PTHR23030; 1.
DR Pfam; PF13949; ALIX_LYPXL_bnd; 1.
DR Pfam; PF03097; BRO1; 1.
DR SMART; SM01041; BRO1; 1.
DR PROSITE; PS51180; BRO1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Cell cycle; Cell division; Cell junction;
KW Cytoplasm; Cytoskeleton; Methylation; Phosphoprotein; Protein transport;
KW Reference proteome; Secreted; Tight junction; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT CHAIN 2..873
FT /note="Programmed cell death 6-interacting protein"
FT /id="PRO_0000349296"
FT DOMAIN 3..397
FT /note="BRO1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT REGION 176..508
FT /note="Interaction with CHMP4A, CHMP4B and CHMP4C"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT REGION 423..873
FT /note="Interaction with SDCBP"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT REGION 508..873
FT /note="Self-association"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT REGION 719..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..725
FT /note="Interaction with TSG101"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT REGION 802..811
FT /note="Interaction with CEP55"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT REGION 837..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..771
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..808
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..873
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT MOD_RES 215
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT MOD_RES 484
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT MOD_RES 742
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT MOD_RES 745
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT MOD_RES 749
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
SQ SEQUENCE 873 AA; 96631 MW; FD7B5D57825D571D CRC64;
MASFIWVQLK KTSEVDLAKP LVKFIQQTYP SGGEEQAQYC RAAEELSKLR RSALGRPLDK
HEGALETLLR YYDQICSIEP KFPFSENQIC LTFTWKDAFD KGSLFGGSVK LALASLGYEK
SCVLFNCAAL ASQIAAEQNL DNDEGLKTAA KQYQFASGAF LHIKDTVLSA LSREPTVDIS
PDTVGTLSLI MLAQAQEVFF LKATRDKMKD AIIAKLANQA ADYFGDAFKQ CQYKDALPKY
FYFQEVFPTL AAKQCIMQAN AEYHQSILAK QQKKFGEEIA RLQHAAELIK NVASRYDEYV
NVKDFSDKIN RALAAAKKDN DFIYHDRVPD LKDLDPIGKA TLVKPTPVNV PISQKFTDLF
EKMVPVSVQQ SLAVFSQRKA DLVNRSIAQM REATTLANGV LASLNLPAAI EDVSGDTVPQ
SILTKSTAVV EQGGIQTVDQ LIKELPELLQ RNREILEESL RLLDEEEATD NDLRAKFKDR
WQRTPSNDLY KPLRAEGAKF RAVLDKAVQA DGQVKERYQS HRDTIALLCK PEPELNAAIP
SANPAKTMQG SEVVNVLKSL LSNLDEIKKE REGLENDLKS VNFDMTSKFL TALAQDGVIN
EEALSVTELD RIYGGLTTKV QESLKKQEGL LKNIQVSHQE FSKMKQSNSE ASLREEVLKN
LATAYDNFVE LVANLKEGTK FYNELTEILV RFQNKCSDIV FARKTERDEL LKDLQQSIAR
EPSAPSIPPP AYQSSPAGGH ATAPTPAPRT MPPAKPQPPA RPPPPVLPAN RVPPAAAATA
PAGVGTASAA PPQTPGSAPP PQAQGPPYPT YPGYPGYCQM PMPMGYNPYT YGQYNMPYPP
VYHQSPGQAP YPGPQQPTYP FPQPPQQSYY PQQ
