FSD1_MOUSE
ID FSD1_MOUSE Reviewed; 496 AA.
AC Q7TPM6; Q3UNE6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Fibronectin type III and SPRY domain-containing protein 1;
GN Name=Fsd1;
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 2).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Diencephalon;
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 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 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 METHYLATION [LARGE SCALE ANALYSIS] AT ARG-310 AND ARG-320, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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 associates 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TPM6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TPM6-2; Sequence=VSP_030767;
CC -!- DOMAIN: B30.2 box contains a microtubule-binding site.
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DR EMBL; AK140132; BAE24249.1; -; mRNA.
DR EMBL; AK144257; BAE25801.1; -; mRNA.
DR EMBL; BC055106; AAH55106.1; -; mRNA.
DR CCDS; CCDS37661.1; -. [Q7TPM6-1]
DR RefSeq; NP_899001.1; NM_183178.2. [Q7TPM6-1]
DR AlphaFoldDB; Q7TPM6; -.
DR BioGRID; 232171; 1.
DR IntAct; Q7TPM6; 1.
DR MINT; Q7TPM6; -.
DR STRING; 10090.ENSMUSP00000011733; -.
DR iPTMnet; Q7TPM6; -.
DR PhosphoSitePlus; Q7TPM6; -.
DR SwissPalm; Q7TPM6; -.
DR MaxQB; Q7TPM6; -.
DR PaxDb; Q7TPM6; -.
DR PeptideAtlas; Q7TPM6; -.
DR PRIDE; Q7TPM6; -.
DR ProteomicsDB; 271640; -. [Q7TPM6-1]
DR ProteomicsDB; 271641; -. [Q7TPM6-2]
DR Antibodypedia; 23560; 201 antibodies from 25 providers.
DR DNASU; 240121; -.
DR Ensembl; ENSMUST00000011733; ENSMUSP00000011733; ENSMUSG00000011589. [Q7TPM6-1]
DR GeneID; 240121; -.
DR KEGG; mmu:240121; -.
DR UCSC; uc008dan.1; mouse. [Q7TPM6-1]
DR CTD; 79187; -.
DR MGI; MGI:1934858; Fsd1.
DR VEuPathDB; HostDB:ENSMUSG00000011589; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000159440; -.
DR HOGENOM; CLU_013137_19_1_1; -.
DR InParanoid; Q7TPM6; -.
DR OMA; TPASWCL; -.
DR OrthoDB; 527460at2759; -.
DR PhylomeDB; Q7TPM6; -.
DR TreeFam; TF333654; -.
DR BioGRID-ORCS; 240121; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Fsd1; mouse.
DR PRO; PR:Q7TPM6; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q7TPM6; protein.
DR Bgee; ENSMUSG00000011589; Expressed in embryonic brain and 158 other tissues.
DR Genevisible; Q7TPM6; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISO:MGI.
DR GO; GO:0051302; P:regulation of cell division; ISO:MGI.
DR GO; GO:0032465; P:regulation of cytokinesis; ISO:MGI.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; ISO:MGI.
DR CDD; cd00063; FN3; 1.
DR CDD; cd12901; SPRY_PRY_FSD1; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003649; Bbox_C.
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 Pfam; PF00041; fn3; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS51262; COS; 1.
DR PROSITE; PS50853; FN3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Methylation; Microtubule; Mitosis; Nucleus;
KW Reference proteome.
FT CHAIN 1..496
FT /note="Fibronectin type III and SPRY domain-containing
FT protein 1"
FT /id="PRO_0000316539"
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 290..477
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REGION 301..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..99
FT /evidence="ECO:0000255"
FT MOD_RES 310
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 320
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 81..97
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030767"
SQ SEQUENCE 496 AA; 55525 MW; A5CBCBDA3015E8FF CRC64;
MEDQREALRK IITTLAMKNE ETQTFIYSLK QMLLNVEANS AKVQEDLEAE FQSLTSVLEE
LKESMLMKIK QDRASRTYEL QNQLAACTRA LESSEELLET ANQTLQASDS EDFSQAAKEI
KDGITMAPAF RLSLKAKVSD NMSHLMVDFA QERQMLQALK FLPVPSAPTI DLAESLVSDN
CVTLVWHMPD EDSKIDHYVL EYRKTNFEGP PRLKEDHPWM VVEGIRQTEH TLTGLKFDMK
YMNIRVKACN KAVAGEFSEP VTLETPAFMF RLDGSTSHQN LRVEDLSAEW DAMGGKVQDI
KAREKEGKGR TASPVNSPAR GTPSPKRMSS GRGGRDRFTA ESYTVLGDTL IDGGEHYWEV
RFEPDSKAFG LGVAYRSLGR FEQLGKTAAS WCLHANNWLQ ASFTAKHANK VKVLDSPVPD
CLGVHCDFHQ GLLSFYNART KQLLHTFKAK FTQPLLPAFT VWCGSFQVTT GLQVPSAVRC
LQKRGSATSS SNTSLT
