ID A0A087V901_BALRE Unreviewed; 656 AA.
AC A0A087V901;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 22-FEB-2023, entry version 23.
DE RecName: Full=Pinin {ECO:0000256|ARBA:ARBA00020056};
DE Flags: Fragment;
GN ORFNames=N312_12158 {ECO:0000313|EMBL:KFO09093.1};
OS Balearica regulorum gibbericeps (East African grey crowned-crane).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Gruidae; Balearica.
OX NCBI_TaxID=100784 {ECO:0000313|EMBL:KFO09093.1, ECO:0000313|Proteomes:UP000053309};
RN [1] {ECO:0000313|EMBL:KFO09093.1, ECO:0000313|Proteomes:UP000053309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N312 {ECO:0000313|EMBL:KFO09093.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00025916}.
CC -!- SUBCELLULAR LOCATION: Cell junction, desmosome
CC {ECO:0000256|ARBA:ARBA00004568}. Nucleus speckle
CC {ECO:0000256|ARBA:ARBA00004324}.
CC -!- SIMILARITY: Belongs to the pinin family.
CC {ECO:0000256|ARBA:ARBA00010386}.
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DR EMBL; KL484366; KFO09093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087V901; -.
DR Proteomes; UP000053309; Unassembled WGS sequence.
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:SF0; PININ; 1.
DR PANTHER; PTHR12707; PINN; 1.
DR Pfam; PF04696; Pinin_SDK_memA; 1.
DR Pfam; PF04697; Pinin_SDK_N; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053309};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 1..95
FT /note="Pinin/SDK"
FT /evidence="ECO:0000259|Pfam:PF04697"
FT DOMAIN 99..224
FT /note="Pinin/SDK/MemA protein"
FT /evidence="ECO:0000259|Pfam:PF04696"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 126..191
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 45..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..592
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO09093.1"
FT NON_TER 656
FT /evidence="ECO:0000313|EMBL:KFO09093.1"
SQ SEQUENCE 656 AA; 73870 MW; BFAB46E2F798CE7F CRC64;
RPPQNRLLAL TGPGGGRGRG SLLLRRGFSD SGGGPPAKQR DLEGASSRLG GERRTRRESR
QESDAEDDDI KKPALPSSVV ATSKERTRRD LIQDQNMDEK GKQRNRRIFG LLMGTLQKFK
QESTVATERQ KRRQEIEQKL EVQAEEERKQ VENERRELFE ERRAKQTELR LLEQKVELAQ
LQEEWNEHNA KIIKYIRTKT KPHLFYIPGR MCPATQKLME ESQKKMNALF ESRRNEFAEQ
INKMEARPRR QSVKEKEQQE VQNEEKKEEQ NKEQEEGKVA QQVEELETGN QHNDVEMEEV
GEEKGKTGSG HSDAEKEQEE DEQTQEMEIK VEETTEVREN DKQQDSQHEE VTVVKEEGEN
IQPVDNEQDV AEMNEADSVE PVENENGKEV EPETVCDAQP EKVCDVPSPE KEKGIKPEIE
AEPEEKQEKA LEAQPEPVAE ALSQPQPVLL PQSPQLSQAA QDPEPQAGKD DSAVVSVKVV
EAQTEQSQTP SVEIKSKTRS RSRGRAGNKT GKSHSRSSSS SSSSSTSSST TSGSSSSTGS
SSSRSSSTTS STTSGSTSRD SSSSSSSSSE SRSRSRGRGH NRDRKRRRST DRKRRDASGV
DRSHKSSKGG SRDTKSSKDK SSRSDRKRSI SESSRSGKRT SRSERDRKSD RKDKRR
//
