SSNA1_BOVIN
ID SSNA1_BOVIN Reviewed; 119 AA.
AC Q5E9C3; Q2NL12;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Microtubule nucleation factor SSNA1 {ECO:0000250|UniProtKB:Q9JJ94};
DE AltName: Full=Sjoegren syndrome nuclear autoantigen 1 homolog;
GN Name=SSNA1 {ECO:0000250|UniProtKB:O43805};
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Microtubule-binding protein which stabilizes dynamic
CC microtubules by slowing growth and shrinkage at both plus and minus
CC ends and serves as a sensor of microtubule damage, protecting
CC microtubules from the microtubule-severing enzyme SPAST (By
CC similarity). Induces microtubule branching which is mediated by the
CC formation of long SSNA1 fibrils which guide microtubule protofilaments
CC to split apart from the mother microtubule and form daughter
CC microtubules (By similarity). Plays a role in axon outgrowth and
CC branching (By similarity). Required for cell division (By similarity).
CC {ECO:0000250|UniProtKB:O43805, ECO:0000250|UniProtKB:Q9XF62}.
CC -!- SUBUNIT: Self-associates to form fibrils. Also forms dimers as well as
CC monomers. Interacts with SPAST. {ECO:0000250|UniProtKB:O43805}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43805}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:O43805}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:O43805}. Midbody {ECO:0000250|UniProtKB:O43805}.
CC Cytoplasm, cytoskeleton, flagellum basal body
CC {ECO:0000250|UniProtKB:O43805}. Cytoplasm, cytoskeleton, flagellum
CC axoneme {ECO:0000250|UniProtKB:O43805}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q9JJ94}. Note=In sperm, strongly expressed in
CC the basal body region with weaker expression in the axoneme (By
CC similarity). Localizes to axon branching points in neurons (By
CC similarity). {ECO:0000250|UniProtKB:O43805,
CC ECO:0000250|UniProtKB:Q9JJ94}.
CC -!- SIMILARITY: Belongs to the SSNA1 family. {ECO:0000305}.
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DR EMBL; BT020997; AAX09014.1; -; mRNA.
DR EMBL; BC111237; AAI11238.1; -; mRNA.
DR RefSeq; NP_001015539.1; NM_001015539.1.
DR AlphaFoldDB; Q5E9C3; -.
DR SMR; Q5E9C3; -.
DR STRING; 9913.ENSBTAP00000054047; -.
DR PaxDb; Q5E9C3; -.
DR PRIDE; Q5E9C3; -.
DR Ensembl; ENSBTAT00000066088; ENSBTAP00000054047; ENSBTAG00000046415.
DR GeneID; 507840; -.
DR KEGG; bta:507840; -.
DR CTD; 8636; -.
DR VEuPathDB; HostDB:ENSBTAG00000046415; -.
DR VGNC; VGNC:35316; SSNA1.
DR eggNOG; ENOG502S16M; Eukaryota.
DR GeneTree; ENSGT00390000012318; -.
DR HOGENOM; CLU_153440_0_0_1; -.
DR InParanoid; Q5E9C3; -.
DR OMA; SYNNELV; -.
DR OrthoDB; 1513306at2759; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000046415; Expressed in spermatocyte and 106 other tissues.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0099512; C:supramolecular fiber; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0140060; P:axon arborization; ISS:UniProtKB.
DR GO; GO:0048675; P:axon extension; ISS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; ISS:UniProtKB.
DR GO; GO:0060830; P:ciliary receptor clustering involved in smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0042073; P:intraciliary transport; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007020; P:microtubule nucleation; IEA:Ensembl.
DR InterPro; IPR033362; SSNA1_fam.
DR PANTHER; PTHR28661; PTHR28661; 1.
PE 3: Inferred from homology;
KW Acetylation; Cell cycle; Cell division; Cell projection; Cilium;
KW Coiled coil; Cytoplasm; Cytoskeleton; Flagellum; Neurogenesis; Nucleus;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43805"
FT CHAIN 2..119
FT /note="Microtubule nucleation factor SSNA1"
FT /id="PRO_0000114482"
FT REGION 2..32
FT /note="Important for localization to the centrosome"
FT /evidence="ECO:0000250|UniProtKB:O43805"
FT COILED 13..70
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:O43805"
SQ SEQUENCE 119 AA; 13599 MW; DFADD4C2331709AD CRC64;
MTQQGAALQN YNNELVKCIE ELCQKREELC RQIQQEEEEK QRLQNEVRQL TEKLARVNEN
LARKIASRNE FDRTIAETEA AYLKILESSQ TLLSVLKREA GNLTKATASE QKSSGGKES
