FCSD1_HUMAN
ID FCSD1_HUMAN Reviewed; 690 AA.
AC Q86WN1; Q6UX75; Q86Y77; Q9NXX8;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=F-BAR and double SH3 domains protein 1;
DE AltName: Full=Protein nervous wreck 2 {ECO:0000250|UniProtKB:Q6PFY1};
DE Short=NWK2 {ECO:0000250|UniProtKB:Q6PFY1};
GN Name=FCHSD1; ORFNames=UNQ737/PRO1431;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Shan Y.X., Yu L.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Blood;
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP INTERACTION WITH 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:0000250|UniProtKB:Q6PFY1}.
CC -!- SUBUNIT: Homodimer. Interacts (via F-BAR domain) with SNX9 (via SH3
CC domain). Interacts (via F-BAR domain) with SNX18 and SNX33. Interacts
CC (via SH3 domain 1) with WASL (By similarity). Interacts (via SH3 domain
CC 2) with ITSN1 (PubMed:29887380). {ECO:0000250|UniProtKB:Q6PFY1,
CC ECO:0000269|PubMed:29887380}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6PFY1}.
CC Perikaryon {ECO:0000250|UniProtKB:Q6PFY1}. Cell projection
CC {ECO:0000250|UniProtKB:Q6PFY1}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q6PFY1}. Note=Detected on neuronal cell bodies
CC and cell projections, in part on cytoplasmic vesicles.
CC {ECO:0000250|UniProtKB:Q6PFY1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86WN1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86WN1-2; Sequence=VSP_023160, VSP_023163;
CC Name=3;
CC IsoId=Q86WN1-3; Sequence=VSP_023161, VSP_023162, VSP_023164,
CC VSP_023165;
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 (By
CC similarity). {ECO:0000250|UniProtKB:O94868,
CC ECO:0000250|UniProtKB:Q6PFY1}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92232.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY217346; AAO45099.1; -; mRNA.
DR EMBL; AY358478; AAQ88842.1; -; mRNA.
DR EMBL; AK000007; BAA92232.1; ALT_INIT; mRNA.
DR EMBL; AC008781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047016; AAH47016.1; -; mRNA.
DR CCDS; CCDS47295.1; -. [Q86WN1-1]
DR RefSeq; NP_258260.1; NM_033449.2. [Q86WN1-1]
DR AlphaFoldDB; Q86WN1; -.
DR SMR; Q86WN1; -.
DR BioGRID; 124619; 26.
DR IntAct; Q86WN1; 9.
DR MINT; Q86WN1; -.
DR STRING; 9606.ENSP00000399259; -.
DR iPTMnet; Q86WN1; -.
DR PhosphoSitePlus; Q86WN1; -.
DR BioMuta; FCHSD1; -.
DR DMDM; 74714119; -.
DR EPD; Q86WN1; -.
DR jPOST; Q86WN1; -.
DR MassIVE; Q86WN1; -.
DR MaxQB; Q86WN1; -.
DR PaxDb; Q86WN1; -.
DR PeptideAtlas; Q86WN1; -.
DR PRIDE; Q86WN1; -.
DR ProteomicsDB; 70181; -. [Q86WN1-1]
DR ProteomicsDB; 70182; -. [Q86WN1-2]
DR ProteomicsDB; 70183; -. [Q86WN1-3]
DR ABCD; Q86WN1; 2 sequenced antibodies.
DR Antibodypedia; 27344; 119 antibodies from 26 providers.
DR DNASU; 89848; -.
DR Ensembl; ENST00000435817.7; ENSP00000399259.2; ENSG00000197948.11. [Q86WN1-1]
DR Ensembl; ENST00000522126.5; ENSP00000427796.1; ENSG00000197948.11. [Q86WN1-3]
DR GeneID; 89848; -.
DR KEGG; hsa:89848; -.
DR MANE-Select; ENST00000435817.7; ENSP00000399259.2; NM_033449.3; NP_258260.1.
DR UCSC; uc003llk.3; human. [Q86WN1-1]
DR CTD; 89848; -.
DR GeneCards; FCHSD1; -.
DR HGNC; HGNC:25463; FCHSD1.
DR HPA; ENSG00000197948; Tissue enhanced (parathyroid).
DR MIM; 617555; gene.
DR neXtProt; NX_Q86WN1; -.
DR OpenTargets; ENSG00000197948; -.
DR PharmGKB; PA134871859; -.
DR VEuPathDB; HostDB:ENSG00000197948; -.
DR eggNOG; KOG3565; Eukaryota.
DR GeneTree; ENSGT00510000046732; -.
DR HOGENOM; CLU_013546_2_0_1; -.
DR InParanoid; Q86WN1; -.
DR OMA; PLDMMVP; -.
DR OrthoDB; 348563at2759; -.
DR PhylomeDB; Q86WN1; -.
DR TreeFam; TF324557; -.
DR PathwayCommons; Q86WN1; -.
DR SignaLink; Q86WN1; -.
DR BioGRID-ORCS; 89848; 6 hits in 1076 CRISPR screens.
DR ChiTaRS; FCHSD1; human.
DR GeneWiki; FCHSD1; -.
DR GenomeRNAi; 89848; -.
DR Pharos; Q86WN1; Tdark.
DR PRO; PR:Q86WN1; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q86WN1; protein.
DR Bgee; ENSG00000197948; Expressed in granulocyte and 100 other tissues.
DR ExpressionAtlas; Q86WN1; baseline and differential.
DR Genevisible; Q86WN1; HS.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0032437; C:cuticular plate; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IBA:GO_Central.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS: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; PF14604; SH3_9; 2.
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..690
FT /note="F-BAR and double SH3 domains protein 1"
FT /id="PRO_0000278212"
FT DOMAIN 12..282
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 468..529
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 546..609
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 422..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 116..149
FT /evidence="ECO:0000255"
FT COILED 354..384
FT /evidence="ECO:0000255"
FT COMPBIAS 422..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..643
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..690
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..320
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_023160"
FT VAR_SEQ 1..76
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023161"
FT VAR_SEQ 77..79
FT /note="SRG -> MDS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023162"
FT VAR_SEQ 321..348
FT /note="GKSGLEKEVQRLTSRAARDYKIQNHGHR -> MQLAKYQSHSKSCPTVFPPT
FT PVLCLPNQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_023163"
FT VAR_SEQ 481..485
FT /note="AGRED -> GVRMS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023164"
FT VAR_SEQ 486..690
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023165"
FT VARIANT 344
FT /note="N -> K (in dbSNP:rs3749760)"
FT /id="VAR_030692"
FT VARIANT 681
FT /note="P -> L (in dbSNP:rs32957)"
FT /id="VAR_030693"
SQ SEQUENCE 690 AA; 76942 MW; EEC9583BCB176897 CRC64;
MQPPPRKVKP AQEVKLRFLE QLSILQTWQQ READLLEDIR SYSKQRAAIE REYGQALQKL
AGPFLKREGH RSGEMDSRGR TVFGAWRCLL DATVAGGQTR LQASDRYRDL AGGTGRSAKE
QVLRKGTENL QRAQAEVLQS VRELSRSRKL YGQRERVWAL AQEKAADVQA RLNRSDHGIF
HSRTSLQKLS TKLSAQSAQY SQQLQAARNE YLLNLVATNA HLDHYYQEEL PALLKALVSE
LSEHLRDPLT SLSHTELEAA EVILEHAHRG EQTTSQVSWE QDLKLFLQEP GVFSPTPPQQ
FQPAGTDQVC VLEWGAEGVA GKSGLEKEVQ RLTSRAARDY KIQNHGHRVL QRLEQRRQQA
SEREAPSIEQ RLQEVRESIR RAQVSQVKGA ARLALLQGAG LDVERWLKPA MTQAQDEVEQ
ERRLSEARLS QRDLSPTAED AELSDFEECE ETGELFEEPA PQALATRALP CPAHVVFRYQ
AGREDELTIT EGEWLEVIEE GDADEWVKAR NQHGEVGFVP ERYLNFPDLS LPESSQDSDN
PCGAEPTAFL AQALYSYTGQ SAEELSFPEG ALIRLLPRAQ DGVDDGFWRG EFGGRVGVFP
SLLVEELLGP PGPPELSDPE QMLPSPSPPS FSPPAPTSVL DGPPAPVLPG DKALDFPGFL
DMMAPRLRPM RPPPPPPAKA PDPGHPDPLT
