PININ_CANLF
ID PININ_CANLF Reviewed; 773 AA.
AC P79149;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Pinin;
GN Name=PNN;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=8922384; DOI=10.1083/jcb.135.4.1027;
RA Ouyang P., Sugrue S.P.;
RT "Characterization of pinin, a novel protein associated with the desmosome-
RT intermediate filament complex.";
RL J. Cell Biol. 135:1027-1042(1996).
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; U77716; AAB48303.1; -; mRNA.
DR AlphaFoldDB; P79149; -.
DR SMR; P79149; -.
DR STRING; 9615.ENSCAFP00000020449; -.
DR PaxDb; P79149; -.
DR eggNOG; KOG3756; Eukaryota.
DR InParanoid; P79149; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0030057; C:desmosome; IDA:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:MGI.
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..773
FT /note="Pinin"
FT /id="PRO_0000190241"
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..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..773
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 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..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..501
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..628
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..708
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..773
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 445
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35691"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 751
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 584
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 592
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 609
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
SQ SEQUENCE 773 AA; 88096 MW; 4A76B191DF80BCBF 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
LFYILGRMCP ATQKLIEESQ RKMNALFEGR RIEFAEQINK MEARPRRQSM KEKEHQVVRN
EEQKAEQEEG KVAQREEELE ETGNQHNDVE IEEAGEEEEK EIGIVHSDAE KEQEEEEQKQ
EMEVKIEEET EVRESEKQQD SQPEEVMDVL EMLLHVAVKN VIAEQEVMET NQVESVEPSE
NETSKELEPE MEFEVEPDKE CKSLSPVREN ASALEMENEP EEKEERESEP QPEPVRHLQP
LPQPEPEPEL QPEPQPQLQP EPQLQPQLQL QLQPQPQSQS QPQPQLQLPL PLPLQPQPQV
QAQSQPQAVL QPQPVSQPET LPLAVLQAPV QVIQEQGHLL PERKEFPVES VKLTEVTVEP
VLIVHSDSKT KTKTRSRSRG RARNKTSKSR SRSSSSSSSS SSSTSSSSGG SSSSGSSSSR
SSSSSSSSTS GSSRRDSSSS TTSSSESRSR SRGRGHNRDR KHRRSVDRKR RDTSGLERSH
KSSKGGSSRD TKGSKDKNSR SDRKRSISES SRSGKRSSRS ERDRKSDRKD KRR
