SPEF1_BOVIN
ID SPEF1_BOVIN Reviewed; 236 AA.
AC Q58DA1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Sperm flagellar protein 1;
GN Name=SPEF1;
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=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Microtubule-associated protein involved in the stabilization
CC of microtubules along the axis of migration during radial
CC intercalation. Promotes the establishment and stabilization of an axis
CC of microtubules required for the active migration of cells into the
CC outer epithelium (By similarity). Microtubule-associated protein that
CC promotes microtubule bundling and stabilizes microtubules against
CC depolymerization in response to cold shock (By similarity). Essential
CC for ciliary central apparatus formation which requires both its
CC microtubule-binding and bundling activities and for ciliary
CC localization of HYDIN and SPAG6 in ependymal cilia (By similarity).
CC Binds actin in intestinal epithelial cells (IECs), essential for IECs
CC survival and contributes to formation of filopodia and lamellipodia in
CC migrating IECs (By similarity). Regulates planar cell polarity
CC signaling pathway and asymmetric microtubule accumulation in ciliated
CC epithelia (By similarity). {ECO:0000250|UniProtKB:Q0IH24,
CC ECO:0000250|UniProtKB:Q99JL1}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with actin, TJP1, CGN and
CC CDH1 (By similarity). {ECO:0000250|UniProtKB:Q99JL1,
CC ECO:0000250|UniProtKB:Q9Y4P9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99JL1}. Cell
CC projection, cilium, flagellum {ECO:0000250|UniProtKB:Q99JL1}.
CC Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q0IH24}.
CC Apical cell membrane {ECO:0000250|UniProtKB:Q0IH24}. Basolateral cell
CC membrane {ECO:0000250|UniProtKB:Q9Y4P9}. Cytoplasm, cytoskeleton,
CC stress fiber {ECO:0000250|UniProtKB:Q9Y4P9}. Cell projection,
CC microvillus {ECO:0000250|UniProtKB:Q9Y4P9}. Cell projection,
CC lamellipodium {ECO:0000250|UniProtKB:Q9Y4P9}. Cell projection,
CC filopodium {ECO:0000250|UniProtKB:Q9Y4P9}. Note=Present in the tails of
CC developing and epididymal sperm, internal to the fibrous sheath and
CC around the outer dense fibers of the sperm flagellum. Also found at the
CC apical tip of cilia. Colocalizes with TJP1 and CGN at sites of cell-
CC cell contact in intestinal epithelial cells (By similarity).
CC {ECO:0000250|UniProtKB:Q0IH24, ECO:0000250|UniProtKB:Q9Y4P9}.
CC -!- DOMAIN: The Calponin-homology domain mediates its binding to
CC microtubules. {ECO:0000250|UniProtKB:Q99JL1}.
CC -!- MISCELLANEOUS: Radial intercalation is a developmentally reiterated
CC form of migration by which cells move in a direction orthogonal to the
CC plane of the tissue from an inner layer to an outer layer.
CC {ECO:0000250|UniProtKB:Q0IH24}.
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DR EMBL; BT021696; AAX46543.1; -; mRNA.
DR EMBL; BC118201; AAI18202.1; -; mRNA.
DR RefSeq; NP_001029594.1; NM_001034422.2.
DR AlphaFoldDB; Q58DA1; -.
DR SMR; Q58DA1; -.
DR STRING; 9913.ENSBTAP00000008640; -.
DR PaxDb; Q58DA1; -.
DR Ensembl; ENSBTAT00000008640; ENSBTAP00000008640; ENSBTAG00000006578.
DR GeneID; 512410; -.
DR KEGG; bta:512410; -.
DR CTD; 25876; -.
DR VEuPathDB; HostDB:ENSBTAG00000006578; -.
DR VGNC; VGNC:35201; SPEF1.
DR eggNOG; ENOG502QRJA; Eukaryota.
DR GeneTree; ENSGT00910000144159; -.
DR HOGENOM; CLU_069635_0_0_1; -.
DR InParanoid; Q58DA1; -.
DR OMA; LYFEVPP; -.
DR OrthoDB; 1471531at2759; -.
DR TreeFam; TF323506; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000006578; Expressed in olfactory segment of nasal mucosa and 90 other tissues.
DR GO; GO:0097729; C:9+2 motile cilium; ISS:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:1990716; C:axonemal central apparatus; ISS:UniProtKB.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0097542; C:ciliary tip; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0005902; C:microvillus; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:1904158; P:axonemal central apparatus assembly; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0003341; P:cilium movement; ISS:UniProtKB.
DR GO; GO:0046847; P:filopodium assembly; ISS:UniProtKB.
DR GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; ISS:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISS:UniProtKB.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IBA:GO_Central.
DR GO; GO:2000095; P:regulation of Wnt signaling pathway, planar cell polarity pathway; ISS:UniProtKB.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR010441; CH_2.
DR InterPro; IPR036872; CH_dom_sf.
DR Pfam; PF06294; CH_2; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Cell membrane; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Flagellum;
KW Membrane; Microtubule; Reference proteome.
FT CHAIN 1..236
FT /note="Sperm flagellar protein 1"
FT /id="PRO_0000254028"
FT DOMAIN 7..112
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 118..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..236
FT /note="Essential for homodimerization and microtubule
FT bundling activity"
FT /evidence="ECO:0000250|UniProtKB:Q99JL1"
SQ SEQUENCE 236 AA; 27111 MW; 0D400F4CA7B76F39 CRC64;
MAGSVDEEAL HQLYLWVDNI PLSRPKRNLS RDFSDGVLVA EVIKFYFPKM VEMHNYVPAN
SLQQKLSNWS HLNRKVLNKL NFSVPEDVMR KIAQCAPGVV ELVLIPLRQR LEERQRRRKQ
GIGSLQELAP QDGTDYMDVG LSQKARGEGV PDPQGRGQLR EGRLPVPRPP GDSQALQSDP
SFILQIAEKE QELLASQETV QVLQMKVRRL EHLLQLKNVR IEDLSRRLQQ AERKQR
