ID A0A2Y9L6X2_ENHLU Unreviewed; 727 AA.
AC A0A2Y9L6X2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Pinin {ECO:0000256|ARBA:ARBA00020056};
GN Name=LOC111161606 {ECO:0000313|RefSeq:XP_022381083.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022381083.1};
RN [1] {ECO:0000313|RefSeq:XP_022381083.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022381083.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_022381083.1; XM_022525375.1.
DR AlphaFoldDB; A0A2Y9L6X2; -.
DR Proteomes; UP000248482; 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: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:UP000248482};
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..132
FT /note="Pinin/SDK"
FT /evidence="ECO:0000259|Pfam:PF04697"
FT DOMAIN 136..260
FT /note="Pinin/SDK/MemA protein"
FT /evidence="ECO:0000259|Pfam:PF04696"
FT REGION 46..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 5..32
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 163..228
FT /evidence="ECO:0000256|SAM:Coils"
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 279..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 402..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..443
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 471..501
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..582
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..662
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 727 AA; 82688 MW; FD937E5FC4DBBAD5 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 EIGIVHSDAE KEQEEEEQKQ
EMEVKMEEET EVRESEKQQD SQPEEVMDVL EMVESVKNVI AEQEVMETNQ VESVEPSENE
TSKELEPEME FEVEPDKECK SLSPVKENAS ALEMENEPEE KEEKESEPQP EPVPEPQPPS
QPQPQLQPPS QPQPPSQPQP QALLQAQPLS QPETLPLAVL QPSIQVFQEQ GHLLPERKEF
PVESVKLTEV TVEPVLTVHS ESKTKTKTRS RSRGRARNKT SKSRSRSSSS SSSSSSSTSS
SSGSSSSSGS SSSRSSSSSS SSTSGSSSRD SSSSTTSSSE SRSRSRGRGH NRDRKHRRSV
DRKRRDTSGL ERSHKSSKGG SSRDTKGSKD KNSRSDRKRS ISESSRSGKR SSRSERDRKS
DRKDKRR
//
