ID FSD1_DANRE Reviewed; 495 AA.
AC Q1LY10;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=Fibronectin type III and SPRY domain-containing protein 1;
GN Name=fsd1; ORFNames=si:ch211-232d19.3;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: May be involved in microtubule organization and
CC stabilization. {ECO:0000250}.
CC -!- SUBUNIT: Oligomerization is required for binding to microtubules.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Cleavage furrow {ECO:0000250}. Note=Cell-cycle-dependent
CC association with the centrosome. Colocalizes with a subpopulation of
CC microtubules. Does not associate with microtubules during mitosis but
CC reassociates with microtubules during cytokinesis. Localizes to the
CC central portions of a small subset of microtubules in interphase cells
CC and a subpopulation of microtubules in the cleavage furrow, not present
CC in the mitotic spindle (By similarity). {ECO:0000250}.
CC -!- DOMAIN: B30.2 box contains a microtubule-binding site.
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DR EMBL; BX247907; CAK04612.1; -; Genomic_DNA.
DR RefSeq; NP_001038582.1; NM_001045117.3.
DR AlphaFoldDB; Q1LY10; -.
DR STRING; 7955.ENSDARP00000083574; -.
DR PaxDb; 7955-ENSDARP00000083574; -.
DR GeneID; 566722; -.
DR KEGG; dre:566722; -.
DR AGR; ZFIN:ZDB-GENE-060503-218; -.
DR CTD; 79187; -.
DR ZFIN; ZDB-GENE-060503-218; fsd1.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; Q1LY10; -.
DR OMA; LETTAFM; -.
DR OrthoDB; 5386672at2759; -.
DR PhylomeDB; Q1LY10; -.
DR PRO; PR:Q1LY10; -.
DR Proteomes; UP000000437; Chromosome 8.
DR Bgee; ENSDARG00000062017; Expressed in brain and 10 other cell types or tissues.
DR ExpressionAtlas; Q1LY10; baseline and differential.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; IMP:ZFIN.
DR GO; GO:0007219; P:Notch signaling pathway; IMP:ZFIN.
DR GO; GO:0051302; P:regulation of cell division; IBA:GO_Central.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IBA:GO_Central.
DR CDD; cd00063; FN3; 1.
DR CDD; cd12901; SPRY_PRY_FSD1; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR035742; SPRY/PRY_FSD1.
DR InterPro; IPR003877; SPRY_dom.
DR PANTHER; PTHR24099; E3 UBIQUITIN-PROTEIN LIGASE TRIM36-RELATED; 1.
DR PANTHER; PTHR24099:SF4; FIBRONECTIN TYPE III AND SPRY DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00622; SPRY; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS51262; COS; 1.
DR PROSITE; PS50853; FN3; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Mitosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..495
FT /note="Fibronectin type III and SPRY domain-containing
FT protein 1"
FT /id="PRO_0000316540"
FT DOMAIN 105..162
FT /note="COS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00586"
FT DOMAIN 164..268
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 281..476
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REGION 306..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..99
FT /evidence="ECO:0000255"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 495 AA; 55876 MW; 4442E71FBD9B71CF CRC64;
MDDQKESLRK IITTLALKNE EIQNFICSLK QSLENLEANS NRVQEDLESE FSSLHSVLDD
LKEGMVTRIK QERASRTYEL QSQLGACTKA LESSEELLEF ANQTLCSSEN DSFTQAAKDI
KDSVTMAPAF RLSLKAKASD SMNHMMVDFT HERNLLQSIT FLPVPATPEI HVADCQVFDN
TVTVVWTLPE PDSKIDHYIL EHRKTNHEGP PRAREDYPWM VVEGIKETEY TLTGVRFDTR
YMTFRVKACN KAVAGEFSEP VTLETHAFVF KLDASSSHQN LKVEDLSVEW DSSGGKVAVQ
DIRKEKNRTN SPMHSPARTA MMSPKRAPSA RVGRDRFTAE SYTVLGDTMI DAGQHYWEVR
FDKESKAFAA GVALRSLGRF DQLGKSNASW CIHLNNWLQQ SLTAKHNNKA RTLDCSIPDR
IGIYCNYEEG TLSFYNSRNK TLLHTFRTKF QQPVIPAFMV WNGSFSVQTG LQVPSIVLSG
QKRNSNTSSS NASLT
//
