ARPIN_XENLA
ID ARPIN_XENLA Reviewed; 227 AA.
AC Q66IV5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Arpin;
GN Name=arpin;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates actin polymerization by inhibiting the actin-
CC nucleating activity of the Arp2/3 complex; the function is competitive
CC with nucleation promoting factors. Involved in steering cell migration
CC by controlling its directional persistence (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Associates with the Arp2/3 complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium {ECO:0000250}.
CC -!- DOMAIN: The acidic C-terminus is necessary and sufficient to inhibit
CC ARP2/3 complex activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Arpin family. {ECO:0000305}.
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DR EMBL; BC081173; AAH81173.1; -; mRNA.
DR RefSeq; NP_001087754.1; NM_001094285.1.
DR AlphaFoldDB; Q66IV5; -.
DR GeneID; 447578; -.
DR KEGG; xla:447578; -.
DR CTD; 447578; -.
DR OMA; HLMSSYK; -.
DR OrthoDB; 1458249at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 447578; Expressed in brain and 19 other tissues.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0033058; P:directional locomotion; ISS:UniProtKB.
DR GO; GO:0051126; P:negative regulation of actin nucleation; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:2000393; P:negative regulation of lamellipodium morphogenesis; ISS:UniProtKB.
DR InterPro; IPR018889; Arpin.
DR PANTHER; PTHR31199; PTHR31199; 1.
DR Pfam; PF10574; UPF0552; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Reference proteome.
FT CHAIN 1..227
FT /note="Arpin"
FT /id="PRO_0000327662"
FT REGION 196..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 227 AA; 25714 MW; 0F63EE377D24D5E8 CRC64;
MSRIYQHTAL QNKPVHDERF DGSWEPGAFQ RGTGVLLEGT LLDFSRHAVT DSKGKKERWY
ILYLRPSKIH RRHFDSKGNE IEPNFSDTKK VNTGFLMSSY KVEAKGESDR ISLEELNRLV
NKVNLMKISE KHTPRETVAF WLPEADMEKT ELELGEQLRV KTMGDGPFLF SLAKVDSGTV
TKCNFAGDAQ AGASWTDNIM ERKSQNTSAP SEPRGQGDGA EDDEWDD