SPEF1_HUMAN
ID SPEF1_HUMAN Reviewed; 236 AA.
AC Q9Y4P9; A5YM71; D3DVY0; Q5JX78;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Sperm flagellar protein 1;
GN Name=SPEF1; Synonyms=C20orf28;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [6]
RP ALTERNATIVE SPLICING.
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 [7]
RP STRUCTURE BY NMR OF 1-120.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CH domain from human sperm flagellar protein
RT 1.";
RL Submitted (AUG-2007) to the PDB data bank.
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP ACTIN; TJP1; CGN AND CDH1.
RX PubMed=31473225; DOI=10.1053/j.gastro.2019.08.031;
RA Tapia R., Perez-Yepez E.A., Carlino M.J., Karandikar U.C., Kralicek S.E.,
RA Estes M.K., Hecht G.A.;
RT "Sperm Flagellar 1 Binds Actin in Intestinal Epithelial Cells and
RT Contributes to Formation of Filopodia and Lamellipodia.";
RL Gastroenterology 157:1544-1555(2019).
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 (PubMed:31473225). 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, ECO:0000269|PubMed:31473225}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with actin, TJP1, CGN and
CC CDH1 (PubMed:31473225). {ECO:0000250|UniProtKB:Q99JL1,
CC ECO:0000269|PubMed:31473225}.
CC -!- INTERACTION:
CC Q9Y4P9; Q6A162: KRT40; NbExp=3; IntAct=EBI-740053, EBI-10171697;
CC Q9Y4P9-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12303571, EBI-3867333;
CC Q9Y4P9-2; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-12303571, EBI-11953846;
CC Q9Y4P9-2; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-12303571, EBI-742388;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:31473225}. Cell
CC projection, cilium, flagellum {ECO:0000250|UniProtKB:Q99JL1}.
CC Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q0IH24}.
CC Apical cell membrane {ECO:0000269|PubMed:31473225}. Basolateral cell
CC membrane {ECO:0000269|PubMed:31473225}. Cytoplasm, cytoskeleton, stress
CC fiber {ECO:0000269|PubMed:31473225}. Cell projection, microvillus
CC {ECO:0000269|PubMed:31473225}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:31473225}. Cell projection, filopodium
CC {ECO:0000269|PubMed:31473225}. Note=Present in the tails of developing
CC and epididymal sperm, internal to the fibrous sheath and around the
CC outer dense fibers of the sperm flagellum. Also found at the apical tip
CC of cilia (By similarity). Colocalizes with TJP1 and CGN at sites of
CC cell-cell contact in intestinal epithelial cells (PubMed:31473225).
CC {ECO:0000250|UniProtKB:Q0IH24, ECO:0000269|PubMed:31473225}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y4P9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y4P9-2; Sequence=VSP_017219, VSP_017220;
CC -!- TISSUE SPECIFICITY: Expressed in the intestinal epithelial cells (at
CC protein level). {ECO:0000269|PubMed:31473225}.
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; AL080154; CAB45745.1; -; mRNA.
DR EMBL; EF560745; ABQ59055.1; -; mRNA.
DR EMBL; AL109804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10503.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10504.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10505.1; -; Genomic_DNA.
DR EMBL; BC022476; AAH22476.1; -; mRNA.
DR CCDS; CCDS13063.2; -. [Q9Y4P9-1]
DR PIR; T12538; T12538.
DR RefSeq; NP_056232.2; NM_015417.4. [Q9Y4P9-1]
DR PDB; 2EE7; NMR; -; A=1-120.
DR PDBsum; 2EE7; -.
DR AlphaFoldDB; Q9Y4P9; -.
DR BMRB; Q9Y4P9; -.
DR SMR; Q9Y4P9; -.
DR BioGRID; 117391; 7.
DR IntAct; Q9Y4P9; 5.
DR STRING; 9606.ENSP00000369080; -.
DR PhosphoSitePlus; Q9Y4P9; -.
DR BioMuta; SPEF1; -.
DR DMDM; 152031688; -.
DR MassIVE; Q9Y4P9; -.
DR PaxDb; Q9Y4P9; -.
DR PeptideAtlas; Q9Y4P9; -.
DR PRIDE; Q9Y4P9; -.
DR ProteomicsDB; 86242; -. [Q9Y4P9-1]
DR ProteomicsDB; 86243; -. [Q9Y4P9-2]
DR Antibodypedia; 62787; 21 antibodies from 11 providers.
DR DNASU; 25876; -.
DR Ensembl; ENST00000379756.3; ENSP00000369080.3; ENSG00000101222.12. [Q9Y4P9-1]
DR GeneID; 25876; -.
DR KEGG; hsa:25876; -.
DR MANE-Select; ENST00000379756.3; ENSP00000369080.3; NM_015417.5; NP_056232.2.
DR UCSC; uc002wjj.4; human. [Q9Y4P9-1]
DR CTD; 25876; -.
DR GeneCards; SPEF1; -.
DR HGNC; HGNC:15874; SPEF1.
DR HPA; ENSG00000101222; Tissue enhanced (brain, choroid plexus, fallopian tube, testis).
DR MIM; 610674; gene.
DR neXtProt; NX_Q9Y4P9; -.
DR OpenTargets; ENSG00000101222; -.
DR PharmGKB; PA162404432; -.
DR VEuPathDB; HostDB:ENSG00000101222; -.
DR eggNOG; ENOG502QRJA; Eukaryota.
DR GeneTree; ENSGT00910000144159; -.
DR HOGENOM; CLU_069635_0_0_1; -.
DR InParanoid; Q9Y4P9; -.
DR OMA; LYFEVPP; -.
DR OrthoDB; 1471531at2759; -.
DR PhylomeDB; Q9Y4P9; -.
DR TreeFam; TF323506; -.
DR PathwayCommons; Q9Y4P9; -.
DR SignaLink; Q9Y4P9; -.
DR BioGRID-ORCS; 25876; 17 hits in 1069 CRISPR screens.
DR EvolutionaryTrace; Q9Y4P9; -.
DR GeneWiki; SPEF1; -.
DR GenomeRNAi; 25876; -.
DR Pharos; Q9Y4P9; Tdark.
DR PRO; PR:Q9Y4P9; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9Y4P9; protein.
DR Bgee; ENSG00000101222; Expressed in right uterine tube and 118 other tissues.
DR Genevisible; Q9Y4P9; HS.
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; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0097542; C:ciliary tip; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0030032; P:lamellipodium assembly; IMP:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; IMP: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 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cell membrane;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Flagellum; Membrane; Microtubule; Reference proteome.
FT CHAIN 1..236
FT /note="Sperm flagellar protein 1"
FT /id="PRO_0000079421"
FT DOMAIN 7..112
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 115..176
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"
FT VAR_SEQ 141..162
FT /note="VSQKARGEGVPDPQGGGQLSWD -> KVAFSISPSRLELSFCPSSCHL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_017219"
FT VAR_SEQ 163..236
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_017220"
FT HELIX 7..19
FT /evidence="ECO:0007829|PDB:2EE7"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:2EE7"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:2EE7"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:2EE7"
FT HELIX 62..75
FT /evidence="ECO:0007829|PDB:2EE7"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:2EE7"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:2EE7"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:2EE7"
FT HELIX 101..116
FT /evidence="ECO:0007829|PDB:2EE7"
SQ SEQUENCE 236 AA; 26987 MW; 74FE1C07D5DE749E CRC64;
MASSVDEEAL HQLYLWVDNI PLSRPKRNLS RDFSDGVLVA EVIKFYFPKM VEMHNYVPAN
SLQQKLSNWG HLNRKVLKRL NFSVPDDVMR KIAQCAPGVV ELVLIPLRQR LEERQRRRKQ
GAGSLQELAP QDGSGYMDVG VSQKARGEGV PDPQGGGQLS WDRPPAPRPP AYNRALQGDP
SFVLQIAEKE QELLASQETV QVLQMKVRRL EHLLQLKNVR IEDLSRRLQQ AERKQR
