PACN1_BOVIN
ID PACN1_BOVIN Reviewed; 444 AA.
AC A7MBI0; A7Z043;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Protein kinase C and casein kinase substrate in neurons protein 1;
GN Name=PACSIN1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal brain, and Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2007) 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 MAPT (By similarity). Interacts (via SH3 domain) with
CC SYNJ1 and WASL. Interacts (via SH3 domain) with DNM1; the interaction
CC is reduced by DNM1 phosphorylation. Interacts with DNM2 and DNM3.
CC Interacts with both COBL and DBNL. Identified in a complex composed of
CC COBL, PACSIN1 and WASL. Interacts with EHD1 and EHD3. Interacts with
CC TRPV4 (By 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 {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=Colocalizes with MAPT in axons. In primary
CC neuronal cultures, present at a high level in presynaptic nerve
CC terminals and in the cell body. Colocalizes with DNM1 at vesicular
CC structures in the cell body and neurites. Associates with membranes via
CC its F-BAR domain (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The F-BAR domain forms a coiled coil and mediates membrane-
CC binding and membrane tubulation. In the autoinhibited conformation,
CC interaction with the SH3 domain inhibits membrane tubulation mediated
CC by the F-BAR domain. DNM1 binding abolishes autoinhibition (By
CC 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; BC151572; AAI51573.1; -; mRNA.
DR EMBL; BC153241; AAI53242.1; -; mRNA.
DR RefSeq; NP_001094571.1; NM_001101101.1.
DR AlphaFoldDB; A7MBI0; -.
DR SMR; A7MBI0; -.
DR STRING; 9913.ENSBTAP00000021459; -.
DR PaxDb; A7MBI0; -.
DR PRIDE; A7MBI0; -.
DR Ensembl; ENSBTAT00000021459; ENSBTAP00000021459; ENSBTAG00000016124.
DR GeneID; 520488; -.
DR KEGG; bta:520488; -.
DR CTD; 29993; -.
DR VEuPathDB; HostDB:ENSBTAG00000016124; -.
DR VGNC; VGNC:32542; PACSIN1.
DR eggNOG; KOG2856; Eukaryota.
DR GeneTree; ENSGT00950000182973; -.
DR HOGENOM; CLU_030752_0_0_1; -.
DR InParanoid; A7MBI0; -.
DR OrthoDB; 727724at2759; -.
DR TreeFam; TF313677; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000016124; Expressed in retina and 86 other tissues.
DR ExpressionAtlas; A7MBI0; baseline.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
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:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0097320; P:plasma membrane tubulation; ISS:UniProtKB.
DR GO; GO:1900006; P:positive regulation of dendrite development; IBA:GO_Central.
DR GO; GO:0072657; P:protein localization to membrane; ISS:UniProtKB.
DR GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
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_0000351649"
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 313..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 26..275
FT /evidence="ECO:0000250"
FT COMPBIAS 332..362
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 108
FT /note="E -> Q (in Ref. 1; AAI53242)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 444 AA; 50658 MW; 96B816669F12EE76 CRC64;
MSGSYDEASL APEETTDSFW EVGNYKRTVK RIDDGHRLCN DLMSCVQERA KIEKAYAQQL
TDWAKRWRQL LEKGPQYGSL ERAWGAIMTE ADKVSELHQE MKNSLLNEDL EKVKNWQKDA
YHKQIMGGFK ETKEAEDGFR KAQKPWAKKM KELEAAKKAY HLACKEEKLA VTREMNSKTE
QSVTPEQQKK LQDKVDKCKQ DVQKTQEKYE KVLDDVGKTT PQYMEGMEQV FEQCQQFEEK
RLVFLKEVLL DIKRHLNLAE SSSYVQVYRE LEQAIRGADA QDDLRWFRST SGPGMPMNWP
QFEEWNPDLP HTAAKKEKQP KKAEGAALTN AAGVVESTSQ AGDRGSVSSY DRGQTYATEW
SDDESGNPFG GSEANGGSNP FDEDAKGVRV RALYDYDGQE QDELSFKAGD ELTKLGEEDE
QGWCRGRLDS GQLGLYPANY VEVV
