PACN1_PONAB
ID PACN1_PONAB Reviewed; 444 AA.
AC Q5R411; Q5R9R0;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Protein kinase C and casein kinase substrate in neurons protein 1;
GN Name=Pacsin1;
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: Binds to membranes via its F-BAR domain and mediates membrane
CC tubulation. Plays a role in the reorganization of the microtubule
CC cytoskeleton via its interaction with MAPT; this decreases microtubule
CC stability and inhibits MAPT-induced microtubule polymerization. Plays a
CC role in cellular transport processes by recruiting DNM1, DNM2 and DNM3
CC to membranes. Plays a role in the reorganization of the actin
CC cytoskeleton and in neuron morphogenesis via its interaction with COBL
CC and WASL, and by recruiting COBL to the cell cortex. Plays a role in
CC the regulation of neurite formation, neurite branching and the
CC regulation of neurite length. Required for normal synaptic vesicle
CC endocytosis; this process retrieves previously released
CC neurotransmitters to accommodate multiple cycles of neurotransmission.
CC Required for normal excitatory and inhibitory synaptic transmission (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. May form heterooligomers with other PACSINs.
CC Interacts with both COBL and DBNL. Identified in a complex composed of
CC COBL, PACSIN1 and WASL. Interacts (via SH3 domain) with SYNJ1 and WASL.
CC Interacts (via SH3 domain) with DNM1; the interaction is reduced by
CC DNM1 phosphorylation. Interacts with DNM2 and DNM3. Interacts with
CC MAPT. Interacts with EHD1 and EHD3. Interacts with TRPV4 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection
CC {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Cell projection,
CC ruffle membrane {ECO:0000250}. Membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Synapse
CC {ECO:0000250}. Cytoplasm, cytosol. Cell membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Note=In primary neuronal cultures, present at a high
CC level in presynaptic nerve terminals and in the cell body. Colocalizes
CC with DNM1 at vesicular structures in the cell body and neurites.
CC Colocalizes with MAPT in axons (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by casein kinase 2 (CK2) and protein kinase C
CC (PKC). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PACSIN family. {ECO:0000305}.
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DR EMBL; CR859322; CAH91500.1; -; mRNA.
DR EMBL; CR861449; CAH93505.1; -; mRNA.
DR RefSeq; NP_001125882.1; NM_001132410.1.
DR RefSeq; XP_009240032.1; XM_009241757.1.
DR AlphaFoldDB; Q5R411; -.
DR SMR; Q5R411; -.
DR STRING; 9601.ENSPPYP00000018470; -.
DR Ensembl; ENSPPYT00000019207; ENSPPYP00000018470; ENSPPYG00000016517.
DR GeneID; 100172814; -.
DR KEGG; pon:100172814; -.
DR CTD; 29993; -.
DR eggNOG; KOG2856; Eukaryota.
DR GeneTree; ENSGT00950000182973; -.
DR HOGENOM; CLU_030752_0_0_1; -.
DR InParanoid; Q5R411; -.
DR OMA; WAAIMTE; -.
DR OrthoDB; 727724at2759; -.
DR TreeFam; TF313677; -.
DR Proteomes; UP000001595; Chromosome 6.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
DR GO; GO:0030137; C:COPI-coated vesicle; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; IEA:Ensembl.
DR GO; GO:0098833; C:presynaptic endocytic zone; IEA:Ensembl.
DR GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0045806; P:negative regulation of endocytosis; IEA:Ensembl.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0097320; P:plasma membrane tubulation; ISS:UniProtKB.
DR GO; GO:0072657; P:protein localization to membrane; ISS:UniProtKB.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISS:UniProtKB.
DR CDD; cd07680; F-BAR_PACSIN1; 1.
DR CDD; cd11998; SH3_PACSIN1-2; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR028518; PACSIN1.
DR InterPro; IPR035743; PACSIN1/PACSIN2_SH3.
DR InterPro; IPR037454; PACSIN1_F-BAR.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23065:SF16; PTHR23065:SF16; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Endocytosis; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; SH3 domain; Synapse; Synaptosome.
FT CHAIN 1..444
FT /note="Protein kinase C and casein kinase substrate in
FT neurons protein 1"
FT /id="PRO_0000351650"
FT DOMAIN 13..283
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 385..444
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 173..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 26..275
FT /evidence="ECO:0000250"
FT COMPBIAS 309..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0W5"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0W5"
FT MOD_RES 184
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0W5"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61644"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61644"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0W5"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61644"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0W5"
FT MOD_RES 394
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q61644"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61644"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61644"
FT CONFLICT 113
FT /note="V -> A (in Ref. 1; CAH91500)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="K -> R (in Ref. 1; CAH91500)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 444 AA; 50922 MW; 2BBE3A6E7374CE49 CRC64;
MSSSYDEASL APEETTDSFW EVGNYKRTVK RIDDGHRLCN DLMNCVQERA KIEKAYGQQL
TDWAKRWRQL IEKGPQYGSL ERAWGAIMTE ADKVSELHQE VKNNLLNEDL EKVKNWQKDA
YHKQIMGGFK ETKEAEDGFR KAQKPWAKKM KELEAAKKAY HLACKEEKLA MTREMNSKSE
QSVTPEQQKK LQDKVDKCKQ DVQKTQEKYE KVLEDVGKTT PQYMENMEQV FEQCQQFEEK
RLVFLKEVLL DIKRHLNLAE NSSYIHVYRE LEQAIRGADA QEDLRWFRST SGPGMPMNWP
QFEEWNPDLP HTTTKKEKQP KKAEGVALTN ATGAVESTSQ AGDRGSVSSY DRGQPYATEW
SDDESGNPFG GSEANGGANP FEDDSKGVRV RALYDYDGQE QDELSFKAGD ELTKLGEEDE
QGWCRGRLDS GQLGLYPANY VEAI
