ID   ARPIN_MOUSE             Reviewed;         226 AA.
AC   Q9D0A3; Q3U1F3; Q8CA84;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Arpin;
DE   AltName: Full=Arp2/3 inhibition protein;
GN   Name=Arpin;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Embryo, Embryonic spinal ganglion, Spinal cord, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Retina;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH ARPC5.
RX   PubMed=24132237; DOI=10.1038/nature12611;
RA   Dang I., Gorelik R., Sousa-Blin C., Derivery E., Guerin C., Linkner J.,
RA   Nemethova M., Dumortier J.G., Giger F.A., Chipysheva T.A., Ermilova V.D.,
RA   Vacher S., Campanacci V., Herrada I., Planson A.G., Fetics S., Henriot V.,
RA   David V., Oguievetskaia K., Lakisic G., Pierre F., Steffen A., Boyreau A.,
RA   Peyrieras N., Rottner K., Zinn-Justin S., Cherfils J., Bieche I.,
RA   Alexandrova A.Y., David N.B., Small J.V., Faix J., Blanchoin L.,
RA   Gautreau A.;
RT   "Inhibitory signalling to the Arp2/3 complex steers cell migration.";
RL   Nature 503:281-284(2013).
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. Participates in an incoherent
CC       feedforward loop at the lamellipodium tip where it inhibits the ARP2/2
CC       complex in response to Rac signaling and where Rac also stimulates
CC       actin polymerization through the WAVE complex. Involved in steering
CC       cell migration by controlling its directional persistence (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Associates with the Arp2/3 complex. Interacts with ARPC2;
CC       enhanced by activated RAC1. Interacts with ARPC5; the interaction is
CC       dependent on RAC1. {ECO:0000269|PubMed:24132237}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium
CC       {ECO:0000269|PubMed:24132237}. Note=Colocalized with the WAVE complex
CC       at lamellipodium tip.
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; AK011654; BAB27760.1; -; mRNA.
DR   EMBL; AK039350; BAC30326.1; -; mRNA.
DR   EMBL; AK051261; BAC34579.1; -; mRNA.
DR   EMBL; AK156013; BAE33545.1; -; mRNA.
DR   EMBL; BC031379; AAH31379.1; -; mRNA.
DR   CCDS; CCDS21390.1; -.
DR   RefSeq; NP_081696.1; NM_027420.4.
DR   AlphaFoldDB; Q9D0A3; -.
DR   SMR; Q9D0A3; -.
DR   BioGRID; 214038; 1.
DR   DIP; DIP-60588N; -.
DR   IntAct; Q9D0A3; 1.
DR   STRING; 10090.ENSMUSP00000049440; -.
DR   iPTMnet; Q9D0A3; -.
DR   PhosphoSitePlus; Q9D0A3; -.
DR   MaxQB; Q9D0A3; -.
DR   PaxDb; Q9D0A3; -.
DR   PeptideAtlas; Q9D0A3; -.
DR   PRIDE; Q9D0A3; -.
DR   ProteomicsDB; 283246; -.
DR   DNASU; 70420; -.
DR   Ensembl; ENSMUST00000048731; ENSMUSP00000049440; ENSMUSG00000039043.
DR   GeneID; 70420; -.
DR   KEGG; mmu:70420; -.
DR   UCSC; uc009hzh.1; mouse.
DR   CTD; 348110; -.
DR   MGI; MGI:1917670; Arpin.
DR   VEuPathDB; HostDB:ENSMUSG00000039043; -.
DR   eggNOG; ENOG502R4IG; Eukaryota.
DR   GeneTree; ENSGT00530000064251; -.
DR   HOGENOM; CLU_106544_0_0_1; -.
DR   InParanoid; Q9D0A3; -.
DR   OMA; HLMSSYK; -.
DR   OrthoDB; 1431350at2759; -.
DR   PhylomeDB; Q9D0A3; -.
DR   BioGRID-ORCS; 70420; 2 hits in 39 CRISPR screens.
DR   PRO; PR:Q9D0A3; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q9D0A3; protein.
DR   Bgee; ENSMUSG00000039043; Expressed in external carotid artery and 215 other tissues.
DR   Genevisible; Q9D0A3; MM.
DR   GO; GO:0030027; C:lamellipodium; IDA: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   1: Evidence at protein level;
KW   Cell projection; Reference proteome.
FT   CHAIN           1..226
FT                   /note="Arpin"
FT                   /id="PRO_0000244266"
FT   REGION          202..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          211..226
FT                   /note="Necessary and sufficient fopr interaction with
FT                   ARPC2"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        49
FT                   /note="I -> V (in Ref. 1; BAE33545)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        85
FT                   /note="F -> L (in Ref. 1; BAC30326)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   226 AA;  25193 MW;  31D7F805E7581345 CRC64;
     MSRIYQDSAL RNKAVQSARL PGTWDPATHQ GGNGILLEGE LVDVSRHSIL DAHGRKERYY
     VLYIQPSCIH RRKFDPKGNE IEPNFSATRK VNTGFLMSSY KVEAKGDTDR LTLEALKSLV
     NKPQLLELTE SLTPDQAVAF WMPESEMEVM ELELGTGVRL KTRGDGPFID SLAKLELGTV
     TKCNFAGDGK TGASWTDNIM AQKSSERNTA EIREQGDGAE DEEWDD