ARP5L_RAT
ID ARP5L_RAT Reviewed; 153 AA.
AC A1L108; Q4KM42;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Actin-related protein 2/3 complex subunit 5-like protein;
DE AltName: Full=Arp2/3 complex 16 kDa subunit 2;
DE Short=ARC16-2;
GN Name=Arpc5l;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Eye;
RX PubMed=8889548; DOI=10.1101/gr.6.9.791;
RA Bonaldo M.F., Lennon G., Soares M.B.;
RT "Normalization and subtraction: two approaches to facilitate gene
RT discovery.";
RL Genome Res. 6:791-806(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 5-153 (ISOFORM 1).
RC TISSUE=Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 90-102 AND 134-145, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May function as component of the Arp2/3 complex which is
CC involved in regulation of actin polymerization and together with an
CC activating nucleation-promoting factor (NPF) mediates the formation of
CC branched actin networks. {ECO:0000250}.
CC -!- SUBUNIT: May be a component of the Arp2/3 complex in which it may
CC replace ARPC5.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A1L108-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A1L108-2; Sequence=VSP_023450;
CC -!- SIMILARITY: Belongs to the ARPC5 family. {ECO:0000305}.
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DR EMBL; BI296526; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC098820; AAH98820.1; -; mRNA.
DR EMBL; BC127445; AAI27446.1; -; mRNA.
DR RefSeq; NP_001032856.2; NM_001037767.2. [A1L108-1]
DR AlphaFoldDB; A1L108; -.
DR SMR; A1L108; -.
DR IntAct; A1L108; 1.
DR MINT; A1L108; -.
DR STRING; 10116.ENSRNOP00000019405; -.
DR iPTMnet; A1L108; -.
DR PhosphoSitePlus; A1L108; -.
DR jPOST; A1L108; -.
DR PaxDb; A1L108; -.
DR PeptideAtlas; A1L108; -.
DR PRIDE; A1L108; -.
DR Ensembl; ENSRNOT00000096562; ENSRNOP00000089031; ENSRNOG00000014317. [A1L108-2]
DR Ensembl; ENSRNOT00000112049; ENSRNOP00000083929; ENSRNOG00000067388. [A1L108-1]
DR GeneID; 296710; -.
DR KEGG; rno:296710; -.
DR UCSC; RGD:1308867; rat. [A1L108-1]
DR CTD; 296710; -.
DR RGD; 1308867; Arpc5l.
DR VEuPathDB; HostDB:ENSRNOG00000014317; -.
DR eggNOG; KOG3380; Eukaryota.
DR GeneTree; ENSGT00940000158501; -.
DR HOGENOM; CLU_101888_1_1_1; -.
DR InParanoid; A1L108; -.
DR OMA; SQIQGRN; -.
DR OrthoDB; 1565115at2759; -.
DR PhylomeDB; A1L108; -.
DR PRO; PR:A1L108; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000014317; Expressed in spleen and 20 other tissues.
DR Genevisible; A1L108; RN.
DR GO; GO:0005885; C:Arp2/3 protein complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR Gene3D; 1.25.40.190; -; 1.
DR InterPro; IPR006789; ARPC5.
DR InterPro; IPR036743; ARPC5_sf.
DR InterPro; IPR030075; ARPC5L.
DR PANTHER; PTHR12644; PTHR12644; 1.
DR PANTHER; PTHR12644:SF2; PTHR12644:SF2; 1.
DR Pfam; PF04699; P16-Arc; 1.
DR PIRSF; PIRSF039096; p16-ARC; 1.
DR SUPFAM; SSF69103; SSF69103; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
FT CHAIN 1..153
FT /note="Actin-related protein 2/3 complex subunit 5-like
FT protein"
FT /id="PRO_0000279483"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023450"
SQ SEQUENCE 153 AA; 17010 MW; 60103D7F18376DCC CRC64;
MARNTLSSRF RRVDIDEFDE NKFVDEHEEA AAASGEPGPD PCEVDGLLRQ GDMLRAFHAA
LRNSPINTKN QAVKERAQGI VLKVLTNFKS SEIEQAVQSL DRNGIDLLMK YIYKGFEKPT
ENSSAVLLQW HEKALAVGGL GSIIRVLTAR KTV
