RUSC1_MOUSE
ID RUSC1_MOUSE Reviewed; 893 AA.
AC Q8BG26; Q6PHT9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=AP-4 complex accessory subunit RUSC1 {ECO:0000305};
DE AltName: Full=New molecule containing SH3 at the carboxy-terminus {ECO:0000303|PubMed:22404429};
DE Short=Nesca {ECO:0000303|PubMed:22404429};
DE AltName: Full=RUN and SH3 domain-containing protein 1;
GN Name=Rusc1 {ECO:0000312|MGI:MGI:1919546};
GN Synonyms=Nesca {ECO:0000303|PubMed:22404429};
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] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Olfactory bulb, and Spinal cord;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ACTIN, TUBB3; STX1A; KIF5B
RP AND KLC1 TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=22404429; DOI=10.1111/j.1471-4159.2012.07729.x;
RA Macdonald J.I., Dietrich A., Gamble S., Hryciw T., Grant R.I., Meakin S.O.;
RT "Nesca, a novel neuronal adapter protein, links the molecular motor kinesin
RT with the pre-synaptic membrane protein, syntaxin-1, in hippocampal
RT neurons.";
RL J. Neurochem. 121:861-880(2012).
CC -!- FUNCTION: Associates with the adapter-like complex 4 (AP-4) and may
CC therefore play a role in vesicular trafficking of proteins at the
CC trans-Golgi network. Signaling adapter which plays a role in neuronal
CC differentiation. Involved in regulation of NGF-dependent neurite
CC outgrowth (By similarity). May play a role in neuronal vesicular
CC trafficking, specifically involving pre-synaptic membrane proteins
CC (PubMed:22404429). Seems to be involved in signaling pathways that are
CC regulated by the prolonged activation of MAPK. Can regulate the
CC polyubiquitination of IKBKG and thus may be involved in regulation of
CC the NF-kappa-B pathway (By similarity). {ECO:0000250|UniProtKB:Q9BVN2,
CC ECO:0000269|PubMed:22404429}.
CC -!- SUBUNIT: Associated component of the adapter-like complex 4 (AP-4) (By
CC similarity). Interacts with IKBKG and TRAF6 (By similarity). Interacts
CC with F-actin, acetylated actin, TUBB3, STX1A, KIF5B and KLC1
CC (PubMed:22404429). {ECO:0000250|UniProtKB:Q9BVN2,
CC ECO:0000269|PubMed:22404429}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22404429}. Nucleus
CC {ECO:0000250|UniProtKB:Q9BVN2}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:22404429}. Cytoplasmic vesicle
CC {ECO:0000305|PubMed:22404429}. Early endosome
CC {ECO:0000305|PubMed:22404429}. Postsynaptic density
CC {ECO:0000269|PubMed:22404429}. Golgi apparatus
CC {ECO:0000305|PubMed:22404429}. Note=Translocated to the nuclear
CC envelope upon stimulation with NGF (By similarity). Associated with
CC membranes and microtubules (PubMed:22404429).
CC {ECO:0000250|UniProtKB:Q9BVN2, ECO:0000269|PubMed:22404429}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BG26-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BG26-2; Sequence=VSP_010856;
CC Name=3;
CC IsoId=Q8BG26-3; Sequence=VSP_010857;
CC -!- TISSUE SPECIFICITY: Expressed in brain, brain stem and spinal cord (at
CC protein level). {ECO:0000269|PubMed:22404429}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 15 dpc in hippocampal, cortical and
CC cerebellar brain, and brain stem and spinal cord. At 18 dpc, expression
CC strongly overlaps with TUBB3 expression in post-mitotic neurons
CC throughout the entire brain. Expression levels increase to 18 dpc/P1
CC after which the levels decline in the hippocampus, cerebellum and brain
CC stem and spinal cord into adulthood while remaining high in the cortex.
CC {ECO:0000269|PubMed:22404429}.
CC -!- DOMAIN: The RUN domain is necessary for NGF induced nuclear
CC redistribution. {ECO:0000250|UniProtKB:Q9BVN2}.
CC -!- PTM: Phosphorylated on serine residues following nuclear translocation.
CC {ECO:0000250|UniProtKB:Q9BVN2}.
CC -!- PTM: Polyubiquitinated; polyubiquitination involves TRAF6.
CC {ECO:0000250|UniProtKB:Q9BVN2}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27820.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC30411.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC31333.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK032334; BAC27820.1; ALT_INIT; mRNA.
DR EMBL; AK039664; BAC30411.1; ALT_INIT; mRNA.
DR EMBL; AK042689; BAC31333.1; ALT_SEQ; mRNA.
DR EMBL; BC056360; AAH56360.1; -; mRNA.
DR EMBL; BC057034; AAH57034.1; -; mRNA.
DR CCDS; CCDS38485.1; -. [Q8BG26-1]
DR CCDS; CCDS38486.1; -. [Q8BG26-3]
DR CCDS; CCDS50956.1; -. [Q8BG26-2]
DR RefSeq; NP_001077276.1; NM_001083807.1. [Q8BG26-1]
DR RefSeq; NP_001077277.1; NM_001083808.1. [Q8BG26-2]
DR RefSeq; NP_082464.2; NM_028188.2. [Q8BG26-3]
DR RefSeq; XP_006502197.1; XM_006502134.3. [Q8BG26-2]
DR AlphaFoldDB; Q8BG26; -.
DR SMR; Q8BG26; -.
DR IntAct; Q8BG26; 5.
DR iPTMnet; Q8BG26; -.
DR PhosphoSitePlus; Q8BG26; -.
DR EPD; Q8BG26; -.
DR MaxQB; Q8BG26; -.
DR PaxDb; Q8BG26; -.
DR PRIDE; Q8BG26; -.
DR ProteomicsDB; 262727; -. [Q8BG26-1]
DR ProteomicsDB; 262728; -. [Q8BG26-2]
DR ProteomicsDB; 262729; -. [Q8BG26-3]
DR Antibodypedia; 34192; 125 antibodies from 23 providers.
DR Ensembl; ENSMUST00000052539; ENSMUSP00000056640; ENSMUSG00000041263. [Q8BG26-1]
DR Ensembl; ENSMUST00000090929; ENSMUSP00000088447; ENSMUSG00000041263. [Q8BG26-3]
DR Ensembl; ENSMUST00000166687; ENSMUSP00000130477; ENSMUSG00000041263. [Q8BG26-2]
DR GeneID; 72296; -.
DR KEGG; mmu:72296; -.
DR UCSC; uc008pxm.1; mouse. [Q8BG26-3]
DR UCSC; uc008pxn.1; mouse. [Q8BG26-1]
DR CTD; 23623; -.
DR MGI; MGI:1919546; Rusc1.
DR VEuPathDB; HostDB:ENSMUSG00000041263; -.
DR eggNOG; ENOG502QWTC; Eukaryota.
DR GeneTree; ENSGT00900000141033; -.
DR HOGENOM; CLU_017252_0_0_1; -.
DR InParanoid; Q8BG26; -.
DR OMA; GWKTNTG; -.
DR OrthoDB; 373320at2759; -.
DR PhylomeDB; Q8BG26; -.
DR TreeFam; TF332235; -.
DR BioGRID-ORCS; 72296; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Rusc1; mouse.
DR PRO; PR:Q8BG26; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8BG26; protein.
DR Bgee; ENSMUSG00000041263; Expressed in motor neuron and 257 other tissues.
DR ExpressionAtlas; Q8BG26; baseline and differential.
DR Genevisible; Q8BG26; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR Gene3D; 1.20.58.900; -; 1.
DR InterPro; IPR004012; Run_dom.
DR InterPro; IPR037213; Run_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF02759; RUN; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00593; RUN; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF140741; SSF140741; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50826; RUN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Endosome; Golgi apparatus; Microtubule; Nucleus; Phosphoprotein;
KW Reference proteome; SH3 domain; Synapse; Ubl conjugation.
FT CHAIN 1..893
FT /note="AP-4 complex accessory subunit RUSC1"
FT /id="PRO_0000097533"
FT DOMAIN 515..659
FT /note="RUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT DOMAIN 835..893
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 31..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..598
FT /note="Interaction with TRAF6"
FT /evidence="ECO:0000250|UniProtKB:Q9BVN2"
FT REGION 599..665
FT /note="Interaction with IKBKG"
FT /evidence="ECO:0000250|UniProtKB:Q9BVN2"
FT REGION 700..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..208
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..402
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..462
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010856"
FT VAR_SEQ 445..446
FT /note="VV -> VAGPSLFPRPPVFRFSADGRPLLEGGGAGAPGSLLFTPLTGWSNSR
FT LRLLGAASPPEEQLLPVRLSPVGAYSPPTRGALPCLASPELALLLSPLFPRSSTFPAAA
FT PLPRQVPAPPLPTPPCPPTAPRWTRRPPPPPRQL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010857"
FT CONFLICT 345
FT /note="P -> Q (in Ref. 1; BAC27820)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 893 AA; 95195 MW; B7CB4102A3CFAAB2 CRC64;
MLSPQRALLC NLNHIHLQHV SLGLHLSRRP ELREGPLSTP PPPGDTGGKE SRGPCSGTLV
DANSNSPAVP CRCCQEHGSS IENQQDPSQE EEAVSPSDPG CSSSLSSCSD LSPDESPVSV
YSRDLPGNED ANPQPSTLEL GSPLAPAGPS TCSPDSFCCS PDSCSGISSP PGPDLDSNCN
ALTTCQDLPS PGLEEEEDSG EQDLATSELS ETEDGRIDAG KAEPSWKINP IWKIDTEKTE
AGWKTIEDSD SGRKTDENTN SSLKTESGKL ASCLNTNSGS KIDAGKTDGG WRGDVSQEPV
PHRTITSFHE LAQKRKRGPG LPLVPQAKKD RSDWLIVFSP DTELPPTGSL GGSLAPPREV
TTFKELRSRS RAQPPPVPPR DPPAGWALVP PRPPPPPVPP RRKKNRLGLQ PIAEGLSEEG
RAASPRAGEE ASASQEPEEP RAHAVVRSSW SFAGVPGAQR LWMAEAQSGT GQLQEQKKGL
LIAVSASVDK IISHFGAARN LVQKAQLGDS RLSPDVGHLV LTTLCPALHA LVADGLKPFR
KDLITGQRRS SPWSVVEASV KPGSCTHSMG SLYSQVSRLA PLSSSRSRFH AFILGLLNTK
QLELWFSSLQ EDAGLLSLLY LPTGFFSLAR GSCPSLATEL LLLLQPLSVL TFHLDLLFEH
HHHLPVGLQQ APAPSCPPPA LQQTMQAVLH WGERLAQSLR GTSGESTTDS STPSARPPAG
SWWDQLTQAS RVYASGGTEG FPLLRWGPRR HGTTAEAAQE APPPTEQTTP GRSVWLGRLF
GVPGCPSETE SGAFKSRRPS SWLPPTVSVL ALVKRGTPPE TPPEALVSSP GSVVQADRAV
RALCDHTAAG PDQLSFQRGE LLRVIATVDE DWLRCGRDGV EGLVPVGYTS LVL
