FCSD1_MOUSE
ID FCSD1_MOUSE Reviewed; 688 AA.
AC Q6PFY1; Q8BV86;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=F-BAR and double SH3 domains protein 1;
DE AltName: Full=Protein nervous wreck 2 {ECO:0000303|PubMed:26567222};
DE Short=NWK2 {ECO:0000303|PubMed:26567222};
GN Name=Fchsd1;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Skin;
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] (ISOFORM 1).
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 IDENTIFICATION.
RX PubMed=15067381;
RA Katoh M., Katoh M.;
RT "Identification and characterization of human FCHSD1 and FCHSD2 genes in
RT silico.";
RL Int. J. Mol. Med. 13:749-754(2004).
RN [4]
RP DOMAIN.
RX PubMed=23761074; DOI=10.1091/mbc.e13-05-0271;
RA Becalska A.N., Kelley C.F., Berciu C., Stanishneva-Konovalova T.B., Fu X.,
RA Wang S., Sokolova O.S., Nicastro D., Rodal A.A.;
RT "Formation of membrane ridges and scallops by the F-BAR protein Nervous
RT Wreck.";
RL Mol. Biol. Cell 24:2406-2418(2013).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH SNX9, AND TISSUE
RP SPECIFICITY.
RX PubMed=23437151; DOI=10.1371/journal.pone.0056516;
RA Cao H., Yin X., Cao Y., Jin Y., Wang S., Kong Y., Chen Y., Gao J.,
RA Heller S., Xu Z.;
RT "FCHSD1 and FCHSD2 are expressed in hair cell stereocilia and cuticular
RT plate and regulate actin polymerization in vitro.";
RL PLoS ONE 8:E56516-E56516(2013).
RN [6]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INTERACTION WITH SNX9; SNX18 AND
RP SNX33, AND DOMAIN.
RX PubMed=26567222; DOI=10.1242/jcs.178699;
RA Ukken F.P., Bruckner J.J., Weir K.L., Hope S.J., Sison S.L.,
RA Birschbach R.M., Hicks L., Taylor K.L., Dent E.W., Gonsalvez G.B.,
RA O'Connor-Giles K.M.;
RT "BAR-SH3 sorting nexins are conserved interacting proteins of Nervous wreck
RT that organize synapses and promote neurotransmission.";
RL J. Cell Sci. 129:166-177(2016).
RN [7]
RP INTERACTION WITH WASL AND ITSN1.
RX PubMed=29887380; DOI=10.1016/j.cell.2018.05.020;
RA Almeida-Souza L., Frank R.A.W., Garcia-Nafria J., Colussi A.,
RA Gunawardana N., Johnson C.M., Yu M., Howard G., Andrews B., Vallis Y.,
RA McMahon H.T.;
RT "A Flat BAR Protein Promotes Actin Polymerization at the Base of Clathrin-
RT Coated Pits.";
RL Cell 174:325-337(2018).
CC -!- FUNCTION: Promotes actin polymerization mediated by SNX9 and WASL.
CC {ECO:0000269|PubMed:23437151}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts (via F-BAR domain) with SNX9
CC (via SH3 domain) (PubMed:23437151, PubMed:26567222). Interacts (via F-
CC BAR domain) with SNX18 and SNX33 (PubMed:26567222). Interacts (via SH3
CC domain 1) with WASL (PubMed:29887380). Interacts (via SH3 domain 2)
CC with ITSN1 (PubMed:29887380). {ECO:0000269|PubMed:23437151,
CC ECO:0000269|PubMed:26567222, ECO:0000269|PubMed:29887380,
CC ECO:0000305|PubMed:23437151}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26567222,
CC ECO:0000305|PubMed:23437151}. Perikaryon {ECO:0000269|PubMed:26567222}.
CC Cell projection {ECO:0000269|PubMed:26567222}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:26567222}. Note=Detected on neuronal cell bodies
CC and cell projections, in part on cytoplasmic vesicles.
CC {ECO:0000269|PubMed:26567222}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PFY1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PFY1-2; Sequence=VSP_023166;
CC -!- TISSUE SPECIFICITY: Detected in inner ear vestibula and in the
CC cuticular plate of cochlear hair cells (at protein level). Ubiquitous.
CC Detected in testis, liver, brain cortex, cerebellum, spiral ganglion
CC and tongue, and at lower levels in the organ of Corti and utricle in
CC the inner ear. {ECO:0000269|PubMed:23437151}.
CC -!- DEVELOPMENTAL STAGE: Detected in brain cortex at 15.5 dpc. Highly
CC expressed in brain cortex from young and adult animals (at protein
CC level). {ECO:0000269|PubMed:26567222}.
CC -!- DOMAIN: The F-BAR domain has an atypical, flat shape and binds
CC preferentially to flat membranes (By similarity). Upon heterologous
CC expression, the isolated F-BAR domain is localized at the cell
CC membrane, and causes the formation of cellular protrusions
CC (PubMed:23761074, PubMed:26567222). {ECO:0000250|UniProtKB:O94868,
CC ECO:0000269|PubMed:23761074, ECO:0000269|PubMed:26567222}.
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DR EMBL; AK079461; BAC37653.1; -; mRNA.
DR EMBL; BC057367; AAH57367.1; -; mRNA.
DR CCDS; CCDS37786.1; -. [Q6PFY1-1]
DR RefSeq; NP_783615.2; NM_175684.4. [Q6PFY1-1]
DR AlphaFoldDB; Q6PFY1; -.
DR SMR; Q6PFY1; -.
DR IntAct; Q6PFY1; 1.
DR STRING; 10090.ENSMUSP00000047878; -.
DR iPTMnet; Q6PFY1; -.
DR PhosphoSitePlus; Q6PFY1; -.
DR EPD; Q6PFY1; -.
DR MaxQB; Q6PFY1; -.
DR PaxDb; Q6PFY1; -.
DR PRIDE; Q6PFY1; -.
DR ProteomicsDB; 271559; -. [Q6PFY1-1]
DR ProteomicsDB; 271560; -. [Q6PFY1-2]
DR Antibodypedia; 27344; 119 antibodies from 26 providers.
DR Ensembl; ENSMUST00000043437; ENSMUSP00000047878; ENSMUSG00000038524. [Q6PFY1-1]
DR GeneID; 319262; -.
DR KEGG; mmu:319262; -.
DR UCSC; uc008ero.1; mouse. [Q6PFY1-1]
DR CTD; 89848; -.
DR MGI; MGI:2441771; Fchsd1.
DR VEuPathDB; HostDB:ENSMUSG00000038524; -.
DR eggNOG; KOG3565; Eukaryota.
DR GeneTree; ENSGT00510000046732; -.
DR HOGENOM; CLU_013546_2_0_1; -.
DR InParanoid; Q6PFY1; -.
DR OMA; PLDMMVP; -.
DR OrthoDB; 348563at2759; -.
DR PhylomeDB; Q6PFY1; -.
DR TreeFam; TF324557; -.
DR BioGRID-ORCS; 319262; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q6PFY1; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q6PFY1; protein.
DR Bgee; ENSMUSG00000038524; Expressed in granulocyte and 80 other tissues.
DR ExpressionAtlas; Q6PFY1; baseline and differential.
DR Genevisible; Q6PFY1; MM.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0061024; P:membrane organization; IMP:GO_Central.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IBA:GO_Central.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:UniProtKB.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR CDD; cd11761; SH3_FCHSD_1; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR034935; FCHSD1.
DR InterPro; IPR035460; FCHSD_SH3_1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15735:SF4; PTHR15735:SF4; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 2.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Lipid-binding; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain.
FT CHAIN 1..688
FT /note="F-BAR and double SH3 domains protein 1"
FT /id="PRO_0000278213"
FT DOMAIN 12..280
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 466..527
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 544..607
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 607..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 360..386
FT /evidence="ECO:0000255"
FT COMPBIAS 610..633
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..688
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WN1"
FT VAR_SEQ 1..259
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023166"
SQ SEQUENCE 688 AA; 76256 MW; 98A9293622D063F2 CRC64;
MQPPPRKVKP AQEVKLRFLE QLSILQTRQQ READLLEDIR SYSKQRAAIE REYGQALQKL
AGPFLKREGQ RSGEADSRTV FGAWRCLLDA TVAGGQTRLQ ASDRYRDLAG GTGRSAKEQV
LRKGTESLQQ AQAEVLQSVR ELSRSRKLYG QRQRVWALAQ EKAADVQARL NRSDHGIFHS
RTSLQKLSTK LSAQSAQYSQ QLRAARNEYL LNLVATNAHL AHYYQEELPA LLKVLVSELS
EYLRDPLTLL GHTELEAAEM ILEHARHGGK ATSQVNWEQD VKLFLQGPGV FSPTPPQQFQ
PAGADQVCGL EWGAGGMAGE SGLEKEVQRW TSRAARDYKI QHHGHRVLQR LEQRRQQAPG
REAPGVEQRL QEVRENIRRA QVSQVKGAAR LALLQEAGLD VQRWLKPAMT QAQDEVEQER
RLSEARLSQR DLSPTAEDAE LSDFDECEEA GELFEEPAPP ALATRPLPCP AHVVFGYQAG
REDELTITEG EWLEVIEEGD ADEWVKARNQ HGEAGFVPER YLNFPDLSLP ESCHGIDNPS
GGEPTAFLAR ALYSYTGQSE EELSFPEGAL IRLLPRAQDG VDDGFWRGEF GGHVGVFPSL
LVEELLGPPG PPELSDPEQM LPSPSPPSFS PPAPTCALDG STAPALPSDK VLDCPGPLDM
MVPRLRPMRP PPPPPAKAPD PGHPDPLT
