FSD1_MACFA
ID FSD1_MACFA Reviewed; 496 AA.
AC Q4R539; Q9BGR6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Fibronectin type III and SPRY domain-containing protein 1;
GN Name=FSD1; ORFNames=QccE-20429, QflA-12963;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Frontal cortex;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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=Q4R539-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4R539-2; Sequence=VSP_030765, VSP_030766;
CC -!- DOMAIN: B30.2 box contains a microtubule-binding site.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE01786.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB056406; BAB33064.1; -; mRNA.
DR EMBL; AB169705; BAE01786.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001271730.1; NM_001284801.1. [Q4R539-1]
DR AlphaFoldDB; Q4R539; -.
DR STRING; 9541.XP_005587618.1; -.
DR GeneID; 101865139; -.
DR CTD; 79187; -.
DR eggNOG; KOG2177; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
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; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 2: Evidence at transcript 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_0000316538"
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 268..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:0000250|UniProtKB:Q7TPM6"
FT MOD_RES 320
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTV5"
FT VAR_SEQ 1..292
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_030765"
FT VAR_SEQ 432..496
FT /note="LLSFYNARTKQVLHTFKTRFTQPLLPAFTVWCGSFQVTTGLQVPSSVRCLQK
FT RGSATSSSNTSLT -> DPKPQLPSLAAP (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_030766"
FT CONFLICT 387
FT /note="T -> A (in Ref. 1; BAB33064)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 496 AA; 55926 MW; 1FC16EB832C1B65C CRC64;
MEEQREALRK IITTLAMKNE EIQSFIYSLK QMLLNVEANS TKVQEDLEAE FQSLFSVLEE
LKEGMLMKIK QDRASRTYEL QNQLAACTRA LESSEELLET ANQTLQAMDR EDFPQAAKQI
KDGVTMAPAF RLSLKAKVSD NMSHLMVDFA QERQMLQALK FLPVPSAPVI DLAESLVADN
CVTLVWRMPD EDSKIDHYVL EYRRTNFEGP PRLKEDQPWM VIEGIRQTEY TLTGLKFDMK
YMNFRVKACN KAVAGEFSEP VTLETPAFMF RLDASTSHQN LRVDDLSVEW DAMGGKVQDI
KAREKDGKGR TASPINSPAR GTPSPKRMPS GRGGRDRFTA ESYTVLGDTL IDGGEHYWEV
RYEPDSKAFG VGVAYRSLGR FEQLGKTAAS WCLHVNNWLQ VSFTAKHANK VKVLDAPVPD
CLGVHCDFHQ GLLSFYNART KQVLHTFKTR FTQPLLPAFT VWCGSFQVTT GLQVPSSVRC
LQKRGSATSS SNTSLT
