SPEF1_XENLA
ID SPEF1_XENLA Reviewed; 229 AA.
AC Q0IH24;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Sperm flagellar protein 1;
GN Name=spef1 {ECO:0000303|PubMed:25070955};
GN Synonyms=clamp {ECO:0000303|PubMed:25070955};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=19767740; DOI=10.1038/ncb1966;
RA Gray R.S., Abitua P.B., Wlodarczyk B.J., Szabo-Rogers H.L., Blanchard O.,
RA Lee I., Weiss G.S., Liu K.J., Marcotte E.M., Wallingford J.B.,
RA Finnell R.H.;
RT "The planar cell polarity effector Fuz is essential for targeted membrane
RT trafficking, ciliogenesis and mouse embryonic development.";
RL Nat. Cell Biol. 11:1225-1232(2009).
RN [3]
RP FUNCTION.
RX PubMed=25070955; DOI=10.1083/jcb.201312045;
RA Werner M.E., Mitchell J.W., Putzbach W., Bacon E., Kim S.K., Mitchell B.J.;
RT "Radial intercalation is regulated by the Par complex and the microtubule-
RT stabilizing protein CLAMP/Spef1.";
RL J. Cell Biol. 206:367-376(2014).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=29514918; DOI=10.1083/jcb.201706058;
RA Kim S.K., Zhang S., Werner M.E., Brotslaw E.J., Mitchell J.W.,
RA Altabbaa M.M., Mitchell B.J.;
RT "CLAMP/Spef1 regulates planar cell polarity signaling and asymmetric
RT microtubule accumulation in the Xenopus ciliated epithelia.";
RL J. Cell Biol. 217:1633-1641(2018).
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 (PubMed:25070955). 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 (By similarity). Regulates
CC planar cell polarity signaling pathway and asymmetric microtubule
CC accumulation in ciliated epithelia (PubMed:29514918).
CC {ECO:0000250|UniProtKB:Q99JL1, ECO:0000269|PubMed:25070955,
CC ECO:0000269|PubMed:29514918}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q99JL1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:19767740}. Apical cell membrane
CC {ECO:0000269|PubMed:29514918}. Note=Also found at the apical tip of
CC cilia. {ECO:0000269|PubMed:19767740}.
CC -!- DOMAIN: The Calponin-homology domain mediates its binding to
CC microtubules. {ECO:0000250|UniProtKB:Q99JL1}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein at the four
CC cell stage results in loss of planar cell polarity protein asymmetry,
CC defects in cilia polarity and affects microtubule asymmetry.
CC {ECO:0000269|PubMed:29514918}.
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:0000305|PubMed:25070955}.
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DR EMBL; BC123353; AAI23354.1; -; mRNA.
DR RefSeq; NP_001090406.1; NM_001096937.1.
DR AlphaFoldDB; Q0IH24; -.
DR SMR; Q0IH24; -.
DR DNASU; 779318; -.
DR GeneID; 779318; -.
DR KEGG; xla:779318; -.
DR CTD; 779318; -.
DR Xenbase; XB-GENE-6252466; spef1.S.
DR OrthoDB; 1471531at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 779318; Expressed in testis and 12 other tissues.
DR GO; GO:0097729; C:9+2 motile cilium; ISS:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:1990716; C:axonemal central apparatus; ISS:UniProtKB.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0097542; C:ciliary tip; 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:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:1904158; P:axonemal central apparatus assembly; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IDA: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:2000095; P:regulation of Wnt signaling pathway, planar cell polarity pathway; IMP: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 Cell membrane; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Cytoplasm; Cytoskeleton; Membrane; Microtubule; Reference proteome.
FT CHAIN 1..229
FT /note="Sperm flagellar protein 1"
FT /id="PRO_0000409220"
FT DOMAIN 7..115
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 122..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..229
FT /note="Essential for homodimerization and microtubule
FT bundling activity"
FT /evidence="ECO:0000250|UniProtKB:Q99JL1"
FT COMPBIAS 122..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 229 AA; 26241 MW; 9417F86FA5B68756 CRC64;
MAVEFDEETM QELYTWVDTI PLSRPKRNIA RDFSDGVLTA ELVKFYFPKL VEMHNYVPAN
STTQKLSNWT ILNRKVLSKL SFSVPDDVIR KIVQCSPGVV ELVLNTLRQK IEEKQRLHHI
SADLSQDQAT QNNGNTHSDK GYKSNGTELS PRQGARVDPA SKTHQGYAQA ANADTTLRFQ
LAEKEQTLIL SQETIQILQA KLRRLEQLLL LKNVRIDDLT RRLQELEKK
