FSD1_BOVIN
ID FSD1_BOVIN Reviewed; 496 AA.
AC Q05B84;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Fibronectin type III and SPRY domain-containing protein 1;
GN Name=FSD1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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 -!- DOMAIN: B30.2 box contains a microtubule-binding site.
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DR EMBL; BC122630; AAI22631.1; -; mRNA.
DR RefSeq; NP_001074987.1; NM_001081518.1.
DR AlphaFoldDB; Q05B84; -.
DR STRING; 9913.ENSBTAP00000007877; -.
DR PaxDb; Q05B84; -.
DR PRIDE; Q05B84; -.
DR Ensembl; ENSBTAT00000077365; ENSBTAP00000066548; ENSBTAG00000005999.
DR GeneID; 510595; -.
DR KEGG; bta:510595; -.
DR CTD; 79187; -.
DR VEuPathDB; HostDB:ENSBTAG00000005999; -.
DR VGNC; VGNC:29129; FSD1.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000159440; -.
DR HOGENOM; CLU_013137_19_1_1; -.
DR InParanoid; Q05B84; -.
DR OrthoDB; 527460at2759; -.
DR TreeFam; TF333654; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000005999; Expressed in Ammon's horn and 65 other tissues.
DR ExpressionAtlas; Q05B84; baseline and differential.
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:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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: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; 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; 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 Pfam; PF00622; SPRY; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
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 Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW Methylation; Microtubule; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..496
FT /note="Fibronectin type III and SPRY domain-containing
FT protein 1"
FT /id="PRO_0000316536"
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"
SQ SEQUENCE 496 AA; 55720 MW; E30FE4104B2B8EF3 CRC64;
MEDQKEALRK IITTLAVKNE EIQSFIYSLK QMLLNVEANS AKVQEDLEAE FQSLFSLLEE
LKEGMLMKIK QDRASRTYEL QNQLAACTRA LESSEELLET ANQTLLATDS KDFPQAAKQI
KDGVTMAPAF RLSLKAKVSD NMSHLMVDFA QERRMLQALT FLPVPSAPVI DLTESLVADN
CVTLVWRMPD EDNKIDHFVL EYRRTNFEGP PRLKEDQPWM VIEGIRQTEY TLTGLKFDMK
YMNFRVKACN KAVSGEFSEP VTLETPAFMF RLDASTSHQN LRVDDLSVEW DAMGGKVQDI
KAREKDGKGR TASPVNSPAR GTPSPKRMPS GRGGRDRFTA ESYTVLGDTL IDGGEHYWEV
RYEPDSKAFG VGVAYRSLGR FEQLGKTAAS WCLHVNNWLQ VSFTAKHANK AKMLDAPVPD
CLGVHCDFHQ GLLSFYNGRT KQLLHTFKAK FTQPLLPAFT VWCGSFHVTT GLQVPSSVRC
LQKRGSATSS SNTSLT
