PININ_PONAB
ID PININ_PONAB Reviewed; 719 AA.
AC Q5R5X0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Pinin;
GN Name=PNN;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional activator binding to the E-box 1 core
CC sequence of the E-cadherin promoter gene; the core-binding sequence is
CC 5'CAGGTG-3'. Capable of reversing CTBP1-mediated transcription
CC repression. Auxiliary component of the splicing-dependent multiprotein
CC exon junction complex (EJC) deposited at splice junction on mRNAs. The
CC EJC is a dynamic structure consisting of core proteins and several
CC peripheral nuclear and cytoplasmic associated factors that join the
CC complex only transiently either during EJC assembly or during
CC subsequent mRNA metabolism. Participates in the regulation of
CC alternative pre-mRNA splicing. Associates to spliced mRNA within 60 nt
CC upstream of the 5'-splice sites. Component of the PSAP complex which
CC binds RNA in a sequence-independent manner and is proposed to be
CC recruited to the EJC prior to or during the splicing process and to
CC regulate specific excision of introns in specific transcription
CC subsets. Involved in the establishment and maintenance of epithelia
CC cell-cell adhesion (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Found in a mRNA splicing-dependent exon junction complex
CC (EJC). Found in a complex with SR proteins. Found in a mRNP complex
CC with RNPS1. Component of the PSAP complex consisting of RNPS1, SAP18
CC and PNN. Interacts with PNISR, CTBP1, CTBP2, KRT8, KRT18, KRT19,
CC PS1D/PNO40, PPIG, RNPS1, SFRS4 and SRRM2. Identified in the spliceosome
CC C complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Cell junction,
CC desmosome {ECO:0000250}. Note=Cell-cell contact area, predominantly
CC desmosome of intercellular adherens junction. Not a nucleocytoplasmic
CC shuttling protein (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pinin family. {ECO:0000305}.
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DR EMBL; CR860732; CAH92846.1; -; mRNA.
DR RefSeq; NP_001126662.1; NM_001133190.1.
DR AlphaFoldDB; Q5R5X0; -.
DR SMR; Q5R5X0; -.
DR STRING; 9601.ENSPPYP00000006552; -.
DR GeneID; 100443066; -.
DR KEGG; pon:100443066; -.
DR CTD; 5411; -.
DR eggNOG; KOG3756; Eukaryota.
DR InParanoid; Q5R5X0; -.
DR OrthoDB; 881609at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR039853; Pinin.
DR InterPro; IPR006786; Pinin_SDK_MemA.
DR InterPro; IPR006787; Pinin_SDK_N.
DR PANTHER; PTHR12707; PTHR12707; 1.
DR Pfam; PF04696; Pinin_SDK_memA; 1.
DR Pfam; PF04697; Pinin_SDK_N; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Cell junction; Coiled coil; DNA-binding;
KW Isopeptide bond; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Spliceosome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CHAIN 2..719
FT /note="Pinin"
FT /id="PRO_0000190244"
FT REGION 46..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..284
FT /note="Sufficient for PSAP complex assembly"
FT /evidence="ECO:0000250"
FT REGION 280..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2..32
FT /evidence="ECO:0000255"
FT COILED 163..234
FT /evidence="ECO:0000255"
FT COILED 287..379
FT /evidence="ECO:0000255"
FT COILED 446..467
FT /evidence="ECO:0000255"
FT COMPBIAS 82..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..574
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 54
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O35691"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 124
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 238
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 238
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O35691"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35691"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 155
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 157
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 157
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 228
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 280
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 304
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 311
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 359
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 365
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 530
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 538
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 555
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
SQ SEQUENCE 719 AA; 81771 MW; 36E83F0CD541E028 CRC64;
MAVAVRTLQE QLEKAKESLK NVDENIRKLT GRDPNDVRPI QARLLALSGP GGGRGRGSLL
LRRGFSDSGG GPPAKQRDLE GAVSRLGGER RTRRESRQES DPEDDDVKKP ALQSSVVATS
KERTRRDLIQ DQNMDEKGKQ RNRRIFGLLM GTLQKFKQES TVATERQKRR QEIEQKLEVQ
AEEERKQVEN ERRELFEERR AKQTELRLLE QKVELAQLQE EWNEHNAKII KYIRTKTKPH
LFYIPGRMCP ATQKLIEESQ RKMNALFEGR RIEFAEQINK MEARPRRQSM KEKEHQVVRN
EEQKAEQEEG KVAQREEELE ETGNQHNDVE IEEAGEEEEK EIAIVHSDAE KEQEEEEQKQ
EIEVKMEEET EVRESEKQQD SQPEEVMDVL EMVENVKHVI ADQEVMETNR VESVEPSENE
ASKELEPEME FEIEPDNECK SLSPGKENVS ALDMEKESEE KEEKESEPQP EPVAQPQPQP
QHQPQLQLQS QSQPVLQSQP PSQPENLSLA VLQPTPQVTQ EQGHLLPERK EFPVESVKLT
EVPVEPVLTV HPESKSKTKT RSRSRGRARN KTSKSRSRSS SSSSSSSSST SSSSGSSSSS
GSSSSRSSSS SSSSTSGSSS RDSSSSTSSS SESRSRSRGR GHNRDRKHRR SVDRKRGDTS
GLERSHKSSK GGSSRDTKGS KDKNSRSDRK RSISESSRSG KRSSRSERDR KSDRKDKRR
