PDC6I_XENLA
ID PDC6I_XENLA Reviewed; 867 AA.
AC Q9W6C5;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Programmed cell death 6-interacting protein;
DE AltName: Full=Signal transduction protein Xp95;
GN Name=pdcd6ip;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PHOSPHORYLATION.
RX PubMed=10026166; DOI=10.1074/jbc.274.9.5522;
RA Che S., El-Hodiri H.M., Wu C.-F., Nelman-Gonzalez M., Weil M.M.,
RA Etkin L.D., Clark R.B., Kuang J.;
RT "Identification and cloning of Xp95, a putative signal transduction protein
RT in Xenopus oocytes.";
RL J. Biol. Chem. 274:5522-5531(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Multifunctional protein that may be 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 that are generated by invagination and scission from the limiting
CC membrane of the endosome (By similarity). Binds to the phospholipid
CC lysobisphosphatidic acid (LBPA) which is abundant in MVBs internal
CC membranes. May play a role in the regulation of both apoptosis and cell
CC proliferation. Regulates exosome biogenesis in concert with SDC1/4 and
CC SDCBP. Ensures 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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9QZA2}. Melanosome
CC {ECO:0000250|UniProtKB:Q8WUM4}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q8WUM4}. Secreted,
CC extracellular exosome {ECO:0000250|UniProtKB:Q8WUM4}. Cell junction,
CC tight junction {ECO:0000250|UniProtKB:Q9WU78}. Midbody, Midbody ring
CC {ECO:0000250|UniProtKB:Q8WUM4}. Note=Component of the actomyosin-tight
CC junction complex (By similarity). {ECO:0000250|UniProtKB:Q9WU78}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9W6C5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9W6C5-2; Sequence=VSP_007503;
CC -!- PTM: Phosphorylated on tyrosine residues.
CC {ECO:0000269|PubMed:10026166}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH43849.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF115497; AAD20341.1; -; mRNA.
DR EMBL; BC043849; AAH43849.1; ALT_INIT; mRNA.
DR RefSeq; NP_001081870.1; NM_001088401.1. [Q9W6C5-1]
DR AlphaFoldDB; Q9W6C5; -.
DR SMR; Q9W6C5; -.
DR BioGRID; 99430; 2.
DR PRIDE; Q9W6C5; -.
DR GeneID; 398095; -.
DR KEGG; xla:398095; -.
DR CTD; 398095; -.
DR Xenbase; XB-GENE-1194427; pdcd6ip.L.
DR OMA; SEWIHHM; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
DR GO; GO:0090543; C:Flemming body; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 Alternative splicing; Cell junction; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Protein transport; Reference proteome; Secreted;
KW Tight junction; Transport.
FT CHAIN 1..867
FT /note="Programmed cell death 6-interacting protein"
FT /id="PRO_0000218894"
FT DOMAIN 3..391
FT /note="BRO1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT REGION 714..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..770
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..867
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 238
FT /note="K -> KYFYFQ (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_007503"
SQ SEQUENCE 867 AA; 96198 MW; 6BE7173E66B263B3 CRC64;
MATFISVPLK KTSEVDLVKP LSKYIHNTYP SGEDQTEYCR AVDELNKLRK SAVGRPLDKH
ETSLETVMRY YDQLCSVEPK FPFTESQLCL TFTWKDAFDK GSIFGGSVKL ALPSLGYEKT
CVLFNIGALA SQIASEQNLD NDEALKAASK FYQLASGAFS HIKDTVLSSL NRDPTVDISP
DTVGTLSLIM LAQAQEVFFL KATRDKMKDA VIAKLANQAA DYYGDAFKQC QYKDTLSKEV
FPILAAKHCI MQAHAEYHQS VLAKQQKKFG EEIGRLQHAS DLVKTVSSRY DEYVNVKDLA
DKINRALTAA KKDNDFIYHD RVPDLKDLDP VGKASLVKST PVNVPLSQKY TDLFEKMVPL
AVQQCLSVYN QRKSELINST IAQMRDATIF ANGVLASLNL PAAVEDVSGD SIPQSILNKS
KTVIEQGGIQ TIGQLIRDLP ELLQRNKEIL EESLKFLDEE EATDNDLKAK FKDRWQRTPS
TELYKPLRSE GSNFRNVLDK AIGADAVVKE RYQSHREAIV ILCKPEAELN AAIPSANPAK
TMQGSEVVTV LKSLLNKLDD MKKEREQLEN DIKSVNFDMT TKFLTALAQD GAVNEEAISV
TELDQIYGSY TYKVQENLKK QEDLLNNIQS AHQEFSKMKQ SNSEANLREE VLKNLAVGHD
NYIELVANLK EGTKFYNDLT DILLKFQCKC SDIVFARKTE RDELLKDIQQ SIAREPSAPS
IPQVPSYQSA PSSISTNIAT SSIPTPAPRT VFSAKQPPPR PPPPAMPSAS PVPASAAQAS
NPAPTAAADS SQPPSNTIPS QAQGPPYPSY PGYPGYYGMP MPVGYNPYMY GQQTIPPYMY
QPPSGQPPYP AQQPSFSYPQ QPFFPPQ
