SPEF1_MOUSE
ID SPEF1_MOUSE Reviewed; 234 AA.
AC Q99JL1; A2ANS9; Q543S5; Q9D4J8;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Sperm flagellar protein 1;
DE AltName: Full=Calponin-homology and microtubule-associated protein {ECO:0000303|PubMed:16206169};
GN Name=Spef1; Synonyms=Clamp {ECO:0000303|PubMed:16206169};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=CD-1; TISSUE=Testis;
RX PubMed=15979255; DOI=10.1016/j.gene.2005.04.025;
RA Chan S.W., Fowler K.J., Choo K.H.A., Kalitsis P.;
RT "Spef1, a conserved novel testis protein found in mouse sperm flagella.";
RL Gene 353:189-199(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Corpus striatum, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16206169; DOI=10.1002/cm.20093;
RA Dougherty G.W., Adler H.J., Rzadzinska A., Gimona M., Tomita Y.,
RA Lattig M.C., Merritt R.C. Jr., Kachar B.;
RT "CLAMP, a novel microtubule-associated protein with EB-type calponin
RT homology.";
RL Cell Motil. Cytoskeleton 62:141-156(2005).
RN [6]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF
RP ARG-31, DISRUPTION PHENOTYPE, AND DOMAIN CALPONIN-HOMOLOGY.
RX PubMed=30535028; DOI=10.1093/jmcb/mjy014;
RA Zheng J., Liu H., Zhu L., Chen Y., Zhao H., Zhang W., Li F., Xie L.,
RA Yan X., Zhu X.;
RT "Microtubule-bundling protein Spef1 enables mammalian ciliary central
RT apparatus formation.";
RL J. Mol. Cell Biol. 11:67-77(2019).
CC -!- FUNCTION: Microtubule-associated protein that promotes microtubule
CC bundling and stabilizes microtubules against depolymerization in
CC response to cold shock (PubMed:16206169). Microtubule-associated
CC protein involved in the stabilization of microtubules along the axis of
CC migration during radial intercalation. Promotes the establishment and
CC stabilization of an axis of microtubules required for the active
CC migration of cells into the outer epithelium (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 (PubMed:30535028).
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:0000269|PubMed:16206169, ECO:0000269|PubMed:30535028}.
CC -!- SUBUNIT: Homodimer (PubMed:30535028). Interacts with actin, TJP1, CGN
CC and CDH1 (By similarity). {ECO:0000250|UniProtKB:Q9Y4P9,
CC ECO:0000269|PubMed:30535028}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15979255}. Cell
CC projection, cilium, flagellum {ECO:0000269|PubMed:15979255}. Cytoplasm,
CC cytoskeleton, cilium axoneme {ECO:0000269|PubMed:30535028}. Apical cell
CC membrane {ECO:0000250|UniProtKB:Q0IH24}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q9Y4P9}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000250|UniProtKB:Q9Y4P9}. Cell projection, microvillus
CC {ECO:0000250|UniProtKB:Q9Y4P9}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q9Y4P9}. Cell projection, filopodium
CC {ECO:0000250|UniProtKB:Q9Y4P9}. Note=Also found at the apical tip of
CC cilia (PubMed:30535028). Present in the tails of developing and
CC epididymal sperm, internal to the fibrous sheath and around the outer
CC dense fibers of the sperm flagellum (PubMed:15979255). Colocalizes with
CC TJP1 and CGN at sites of cell-cell contact in intestinal epithelial
CC cells (By similarity). {ECO:0000250|UniProtKB:Q9Y4P9,
CC ECO:0000269|PubMed:15979255, ECO:0000269|PubMed:30535028}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the seminiferous
CC epithelium of adult testis (PubMed:15979255). Expressed in pillar cells
CC of the organ of Corti (at protein level). Expressed in brain, kidney,
CC lung and testis (PubMed:16206169, PubMed:30535028). Highly expressed in
CC the trachea, lung and oviduct (PubMed:30535028).
CC {ECO:0000269|PubMed:15979255, ECO:0000269|PubMed:16206169,
CC ECO:0000269|PubMed:30535028}.
CC -!- DEVELOPMENTAL STAGE: Expression is first detected in the testis at 3
CC weeks and continues to adulthood. {ECO:0000269|PubMed:15979255}.
CC -!- DOMAIN: The Calponin-homology domain mediates its binding to
CC microtubules. {ECO:0000269|PubMed:30535028}.
CC -!- DISRUPTION PHENOTYPE: Depletion in ependymal cells by RNAi completely
CC abolishes the central pair microtubules and markedly attenuates ciliary
CC localizations of HYDIN and SPAG6, resulting in rotational beat of the
CC ependymal cilia. {ECO:0000269|PubMed:30535028}.
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; AY860964; AAX56299.1; -; mRNA.
DR EMBL; AK016476; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK046964; BAC32928.1; -; mRNA.
DR EMBL; AK047675; BAC33121.1; -; mRNA.
DR EMBL; AL831736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006046; AAH06046.1; -; mRNA.
DR CCDS; CCDS38245.1; -.
DR RefSeq; NP_081917.1; NM_027641.2.
DR AlphaFoldDB; Q99JL1; -.
DR SMR; Q99JL1; -.
DR STRING; 10090.ENSMUSP00000105847; -.
DR iPTMnet; Q99JL1; -.
DR PhosphoSitePlus; Q99JL1; -.
DR MaxQB; Q99JL1; -.
DR PaxDb; Q99JL1; -.
DR PRIDE; Q99JL1; -.
DR ProteomicsDB; 261569; -.
DR Antibodypedia; 62787; 21 antibodies from 11 providers.
DR DNASU; 70997; -.
DR Ensembl; ENSMUST00000028801; ENSMUSP00000028801; ENSMUSG00000027329.
DR Ensembl; ENSMUST00000110218; ENSMUSP00000105847; ENSMUSG00000027329.
DR GeneID; 70997; -.
DR KEGG; mmu:70997; -.
DR UCSC; uc008mkv.1; mouse.
DR CTD; 25876; -.
DR MGI; MGI:3513546; Spef1.
DR VEuPathDB; HostDB:ENSMUSG00000027329; -.
DR eggNOG; ENOG502S497; Eukaryota.
DR GeneTree; ENSGT00910000144159; -.
DR HOGENOM; CLU_069635_0_0_1; -.
DR InParanoid; Q99JL1; -.
DR OMA; LYFEVPP; -.
DR OrthoDB; 1471531at2759; -.
DR PhylomeDB; Q99JL1; -.
DR TreeFam; TF323506; -.
DR BioGRID-ORCS; 70997; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q99JL1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q99JL1; protein.
DR Bgee; ENSMUSG00000027329; Expressed in ileal epithelium and 154 other tissues.
DR ExpressionAtlas; Q99JL1; baseline and differential.
DR Genevisible; Q99JL1; MM.
DR GO; GO:0097729; C:9+2 motile cilium; IDA:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:1990716; C:axonemal central apparatus; IDA: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; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
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:0031514; C:motile cilium; IDA:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:1904158; P:axonemal central apparatus assembly; IMP:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0003341; P:cilium movement; IMP: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; IDA:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; ISS:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA: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 1: Evidence at protein level;
KW Actin-binding; Cell membrane; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Flagellum;
KW Membrane; Microtubule; Reference proteome.
FT CHAIN 1..234
FT /note="Sperm flagellar protein 1"
FT /id="PRO_0000079422"
FT DOMAIN 7..112
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 181..234
FT /note="Essential for homodimerization and microtubule
FT bundling activity"
FT /evidence="ECO:0000269|PubMed:30535028"
FT MUTAGEN 31
FT /note="R->A: Disruption of its microtubule-binding and
FT microtubule bundling activities. Failure to rescue ciliary
FT central apparatus formation in SPEF1-depleted ependymal
FT cilia."
FT /evidence="ECO:0000269|PubMed:30535028"
FT CONFLICT 111
FT /note="L -> P (in Ref. 2; AK016476)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="P -> L (in Ref. 2; AK016476)"
FT /evidence="ECO:0000305"
FT CONFLICT 187..233
FT /note="KEQELLASQETVQVLQMKVKRLEHLLQLKNVRIDDLSRRLQQAERKQ -> R
FT SRSCWPLKRQYRSF (in Ref. 2; AK016476)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 234 AA; 26839 MW; 1772A71278845F44 CRC64;
MESSVDEEAL HQLYLWVDNI PLSRPKRNLS RDFSDGVLVA ELIKFYFPKM VEMHNYVPAN
SLQQKLSNWG HLNRKVLNKL NFSVPDDVMR KIAQCSPGVV ELVLIPLRQR LEERQRRQKL
GVGSLQELAP QDSSGYMDMG LPQKVRGEGA PALGEQLREG RPLASRPPGY NQALQGDPSF
VLQIAEKEQE LLASQETVQV LQMKVKRLEH LLQLKNVRID DLSRRLQQAE RKQR
