ID A0A9D3PNF5_MEGAT Unreviewed; 612 AA.
AC A0A9D3PNF5;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 02-APR-2025, entry version 7.
DE RecName: Full=Pinin {ECO:0000256|ARBA:ARBA00020056};
GN ORFNames=MATL_G00208170 {ECO:0000313|EMBL:KAG7461262.1};
OS Megalops atlanticus (Tarpon) (Clupea gigantea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Elopiformes; Megalopidae; Megalops.
OX NCBI_TaxID=7932 {ECO:0000313|EMBL:KAG7461262.1, ECO:0000313|Proteomes:UP001046870};
RN [1] {ECO:0000313|EMBL:KAG7461262.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YG-15Mar2019-1 {ECO:0000313|EMBL:KAG7461262.1};
RC TISSUE=Brain {ECO:0000313|EMBL:KAG7461262.1};
RA Zahm M., Roques C., Cabau C., Klopp C., Donnadieu C., Jouanno E.,
RA Lampietro C., Louis A., Herpin A., Echchiki A., Berthelot C., Parey E.,
RA Roest-Crollius H., Braasch I., Postlethwait J., Bobe J., Montfort J.,
RA Bouchez O., Begum T., Mejri S., Adams A., Chen W.-J., Guiguen Y.;
RL Submitted (JAN-2021) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAG7461262.1}.
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DR EMBL; JAFDVH010000018; KAG7461262.1; -; Genomic_DNA.
DR OrthoDB; 330772at2759; -.
DR Proteomes; UP001046870; Chromosome 18.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IEA:TreeGrafter.
DR GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
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:UP001046870};
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 16..148
FT /note="Pinin/SDK"
FT /evidence="ECO:0000259|Pfam:PF04697"
FT DOMAIN 152..277
FT /note="Pinin/SDK/MemA protein"
FT /evidence="ECO:0000259|Pfam:PF04696"
FT REGION 40..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 179..237
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 40..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..369
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..397
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..606
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 612 AA; 67619 MW; 48A39ACE4AC88F37 CRC64;
MLCGGEGERS PERTKMAVAV RTLQDQLEKA KESLKNVDEN IRKLTGRDPN ELRPGQARRL
TIAGLGGGRG RGINLLRRGL SDSGGGPPAK QRDIEGALLR LAGDQRARRD SRHDSDADDD
DDVKKPALQS SVVATSKERT RRDLIQDQTM DEKGKQRNRR MFGLLMGTLQ KFKQESTVAT
EKEKRRQEIE QKLEVQAEQE RKKVESERRE LFEERRAKQT ELRLLEQKVE LAQLQEEWNV
HNAKIIKYIR TKTKPPIFYI PGRMCSATHK LLEESQKKMN AMFEERQVEF AEQLNKMEAR
PRRQAMRDRE QEANQSEEPK REEQAEGKPS GQEAETGNRE DVEMEEAGEE VSVAQSDGEQ
AAEEEEEEER AGQEQARRAE ASKEDEEDEE DEEEDVGQAE GREVEERVAA AEAGHAEREQ
PADGGLQAEE ATGREQESPE AVEMEVGNGG RESGEAEGEK EPPADPRQES AAESEGQENG
VETQSTASKQ QQLQPPEAME TEPGAEVRVA PASETQPLPE GSGAERPAPT EAAHPERESQ
PQPDAKPKAA GVPGEGRGRG TVRDRKKSRS SSSSSSSSSS SSSGSSSSGS SSSGSSSSSS
TSSSSRSRAR WR
//
