A7MBI0 (PACN1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein kinase C and casein kinase substrate in neurons protein 1

Gene names

Name:

PACSIN1

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	444 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Binds to membranes via its F-BAR domain and mediates membrane tubulation. Plays a role in the reorganization of the microtubule cytoskeleton via its interaction with MAPT; this decreases microtubule stability and inhibits MAPT-induced microtubule polymerization. Plays a role in cellular transport processes by recruiting DNM1, DNM2 and DNM3 to membranes. Plays a role in the reorganization of the actin cytoskeleton and in neuron morphogenesis via its interaction with COBL and WASL, and by recruiting COBL to the cell cortex. Plays a role in the regulation of neurite formation, neurite branching and the regulation of neurite length. Required for normal synaptic vesicle endocytosis; this process retrieves previously released neurotransmitters to accomodate multiple cycles of neurotransmission. Required for normal excitatory and inhibitory synaptic transmission By similarity.
Subunit structure	Homodimer. May form heterooligomers with other PACSINs. Interacts with MAPT By similarity. Interacts (via SH3 domain) with SYNJ1 and WASL. Interacts (via SH3 domain) with DNM1; the interaction is reduced by DNM1 phosphorylation. Interacts with DNM2 and DNM3. Interacts with both COBL and DBNL. Identified in a complex composed of COBL, PACSIN1 and WASL. Interacts with EHD1 and EHD3 By similarity.
Subcellular location	Cytoplasm By similarity. Cell projection By similarity. Cell junction › synapse › synaptosome By similarity. Cell projection › ruffle membrane By similarity. Membrane; Peripheral membrane protein By similarity. Cytoplasmic vesicle membrane; Peripheral membrane protein By similarity. Cell junction › synapse By similarity. Cytoplasm › cytosol By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Colocalizes with MAPT in axons. In primary neuronal cultures, present at a high level in presynaptic nerve terminals and in the cell body. Colocalizes with DNM1 at vesicular structures in the cell body and neurites. Associates with membranes via its F-BAR domain By similarity.
Domain	The F-BAR domain forms a coiled coil and mediates membrane-binding and membrane tubulation. In the autoinhibited conformation, interaction with the SH3 domain inhibits membrane tubulation mediated by the F-BAR domain. DNM1 binding abolishes autoinhibition By similarity.
Post-translational modification	Phosphorylated by casein kinase 2 (CK2) and protein kinase C (PKC) Probable.
Sequence similarities	Belongs to the PACSIN family. Contains 1 FCH domain. Contains 1 SH3 domain.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Cytoplasmic vesicle Membrane Synapse Synaptosome
Domain	Coiled coil SH3 domain
Ligand	Lipid-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	membrane tubulation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of endocytosis Inferred from electronic annotation. Source: Compara neuron projection morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB protein localization to membrane Inferred from sequence or structural similarity. Source: UniProtKB synaptic vesicle endocytosis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	COPI-coated vesicle Inferred from electronic annotation. Source: Compara axon terminus Inferred from sequence or structural similarity. Source: UniProtKB cell junction Inferred from electronic annotation. Source: UniProtKB-KW cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB cytoplasmic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell ruffle membrane Inferred from sequence or structural similarity. Source: UniProtKB synapse Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	phospholipid binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 444	444	Protein kinase C and casein kinase substrate in neurons protein 1		PRO_0000351649
Regions
	Domain	13 – 76	64	FCH
	Domain	385 – 444	60	SH3
	Region	1 – 307	307	F-BAR domain By similarity
	Coiled coil	26 – 275	250	By similarity
Amino acid modifications
	Modified residue	79	1	Phosphoserine By similarity
	Modified residue	184	1	Phosphothreonine By similarity
	Modified residue	394	1	Phosphotyrosine By similarity
Experimental info
	Sequence conflict	108	1	E → Q in AAI53242. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	A7MBI0 [UniParc]. Last modified October 2, 2007. Version 1. Checksum: 96B816669F12EE76	FASTA	444	50,658
	10 20 30 40 50 60 MSGSYDEASL APEETTDSFW EVGNYKRTVK RIDDGHRLCN DLMSCVQERA KIEKAYAQQL 70 80 90 100 110 120 TDWAKRWRQL LEKGPQYGSL ERAWGAIMTE ADKVSELHQE MKNSLLNEDL EKVKNWQKDA 130 140 150 160 170 180 YHKQIMGGFK ETKEAEDGFR KAQKPWAKKM KELEAAKKAY HLACKEEKLA VTREMNSKTE 190 200 210 220 230 240 QSVTPEQQKK LQDKVDKCKQ DVQKTQEKYE KVLDDVGKTT PQYMEGMEQV FEQCQQFEEK 250 260 270 280 290 300 RLVFLKEVLL DIKRHLNLAE SSSYVQVYRE LEQAIRGADA QDDLRWFRST SGPGMPMNWP 310 320 330 340 350 360 QFEEWNPDLP HTAAKKEKQP KKAEGAALTN AAGVVESTSQ AGDRGSVSSY DRGQTYATEW 370 380 390 400 410 420 SDDESGNPFG GSEANGGSNP FDEDAKGVRV RALYDYDGQE QDELSFKAGD ELTKLGEEDE 430 440 QGWCRGRLDS GQLGLYPANY VEVV

References

[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Fetal brain and Fetal skin.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC151572 mRNA. Translation: AAI51573.1. BC153241 mRNA. Translation: AAI53242.1.
IPI	IPI00713676.
RefSeq	NP_001094571.1. NM_001101101.1.
UniGene	Bt.35936.
3D structure databases
ProteinModelPortal	A7MBI0.
ModBase	Search...
Protein-protein interaction databases
STRING	9913.ENSBTAP00000021459.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000021459; ENSBTAP00000021459; ENSBTAG00000016124.
GeneID	520488.
KEGG	bta:520488.
Organism-specific databases
CTD	29993.
Phylogenomic databases
eggNOG	NOG283356.
GeneTree	ENSGT00510000046376.
HOGENOM	HOG000007245.
HOVERGEN	HBG053486.
InParanoid	A7MBI0.
OMA	PDSLGWC.
OrthoDB	EOG4QVCC5.
Family and domain databases
InterPro	IPR001060. FCH_dom. IPR001452. SH3_domain. [Graphical view]
Pfam	PF00611. FCH. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00452. SH3DOMAIN.
SMART	SM00055. FCH. 1 hit. SM00326. SH3. 1 hit. [Graphical view]
SUPFAM	SSF50044. SH3. 1 hit.
PROSITE	PS50133. FCH. 1 hit. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20873115.

Entry information

Entry name

PACN1_BOVIN

Accession

Primary (citable) accession number: A7MBI0
Secondary accession number(s): A7Z043

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 14, 2008
Last sequence update:	October 2, 2007
Last modified:	May 29, 2013
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program