ID   SPAG1_DANRE             Reviewed;         427 AA.
AC   F1RBN2; A4QNV4;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Sperm-associated antigen 1A;
GN   Name=spag1a; Synonyms=spag1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 32-427.
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24055112; DOI=10.1016/j.ajhg.2013.07.025;
RA   Knowles M.R., Ostrowski L.E., Loges N.T., Hurd T., Leigh M.W., Huang L.,
RA   Wolf W.E., Carson J.L., Hazucha M.J., Yin W., Davis S.D., Dell S.D.,
RA   Ferkol T.W., Sagel S.D., Olivier K.N., Jahnke C., Olbrich H., Werner C.,
RA   Raidt J., Wallmeier J., Pennekamp P., Dougherty G.W., Hjeij R., Gee H.Y.,
RA   Otto E.A., Halbritter J., Chaki M., Diaz K.A., Braun D.A., Porath J.D.,
RA   Schueler M., Baktai G., Griese M., Turner E.H., Lewis A.P., Bamshad M.J.,
RA   Nickerson D.A., Hildebrandt F., Shendure J., Omran H., Zariwala M.A.;
RT   "Mutations in SPAG1 cause primary ciliary dyskinesia associated with
RT   defective outer and inner dynein arms.";
RL   Am. J. Hum. Genet. 93:711-720(2013).
CC   -!- FUNCTION: May play a role in the cytoplasmic assembly and/or
CC       trafficking of the axonemal dynein arms. {ECO:0000269|PubMed:24055112}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q07617}. Dynein
CC       axonemal particle {ECO:0000250|UniProtKB:Q07617}. Note=Colocalizes with
CC       tubulin. {ECO:0000250|UniProtKB:Q07617}.
CC   -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
CC       increase incidence of dorsal curvature and hydrocephalus.
CC       {ECO:0000269|PubMed:24055112}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI39536.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; FP236813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC139535; AAI39536.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; F1RBN2; -.
DR   SMR; F1RBN2; -.
DR   STRING; 7955.ENSDARP00000104892; -.
DR   PaxDb; F1RBN2; -.
DR   PRIDE; F1RBN2; -.
DR   Ensembl; ENSDART00000185960; ENSDARP00000154012; ENSDARG00000004017.
DR   ZFIN; ZDB-GENE-030131-9443; spag1a.
DR   eggNOG; KOG1124; Eukaryota.
DR   GeneTree; ENSGT00940000154697; -.
DR   HOGENOM; CLU_061396_0_0_1; -.
DR   InParanoid; F1RBN2; -.
DR   PhylomeDB; F1RBN2; -.
DR   TreeFam; TF106202; -.
DR   PRO; PR:F1RBN2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 19.
DR   Bgee; ENSDARG00000004017; Expressed in granulocyte and 35 other tissues.
DR   ExpressionAtlas; F1RBN2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0120293; C:dynein axonemal particle; IEA:UniProtKB-SubCell.
DR   GO; GO:0070286; P:axonemal dynein complex assembly; IMP:UniProtKB.
DR   Gene3D; 1.25.40.10; -; 2.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR001440; TPR_1.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF00515; TPR_1; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00028; TPR; 6.
DR   SUPFAM; SSF48452; SSF48452; 2.
DR   PROSITE; PS50005; TPR; 6.
DR   PROSITE; PS50293; TPR_REGION; 2.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Reference proteome; Repeat; TPR repeat.
FT   CHAIN           1..427
FT                   /note="Sperm-associated antigen 1A"
FT                   /id="PRO_0000428751"
FT   REPEAT          125..158
FT                   /note="TPR 1"
FT   REPEAT          167..200
FT                   /note="TPR 2"
FT   REPEAT          202..234
FT                   /note="TPR 3"
FT   REPEAT          302..335
FT                   /note="TPR 4"
FT   REPEAT          336..369
FT                   /note="TPR 5"
FT   REPEAT          371..403
FT                   /note="TPR 6"
FT   REGION          46..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        105
FT                   /note="P -> L (in Ref. 2; AAI39536)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   427 AA;  46984 MW;  AC631ED75F2C51E8 CRC64;
     MSQQEVCPLN LFQSAQGTGR VCMRVCVCER GRELAVLYRA AMGNAQKKGP GYREGGGPNS
     QPGTPGRRRS HGLNNAANSK EVPGSSPAAN GSLPAGKSQD EPQGPGSAGE SCNLDAPCGA
     LPPPLARLKN QGNMLFKNGQ FGDALEKYTQ AIDGCIEAGI DSPEDLCVLY SNRAACFLKD
     GNSADCIQDC TRALELHPFS LKPLLRRAMA YESLERYRKA YVDYKTVLQI DISVQAAHDS
     VHRITKMLIE QDGPDWREKL PEIPAVPLSA QQHRKEEPSA ELLQARAERA EQEKARKAEA
     RFTILKQEGN ELVKNSQFQG ASEKYSECLA IKPNECAIYT NRALCFLKLE RFAEAKQDCD
     SALQMEPKNK KAFYRRALAH KGLKDYLSAS TDLQEVLQLD PNVQEAEQEL EMVTNLLRES
     LLANAQG