ODFP2_MOUSE
ID ODFP2_MOUSE Reviewed; 830 AA.
AC A3KGV1; A3KGV5; A3KGV6; O35135; O35496; Q3TH68; Q3UP80; Q6PGI6;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Outer dense fiber protein 2;
DE AltName: Full=84 kDa outer dense fiber protein;
DE AltName: Full=Cenexin;
DE AltName: Full=Outer dense fiber of sperm tails protein 2;
GN Name=Odf2; Synonyms=Odf84;
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] (ISOFORMS 6 AND 7), TISSUE SPECIFICITY, AND
RP ALTERNATIVE SPLICING.
RC TISSUE=Sperm;
RX PubMed=9740324;
RX DOI=10.1002/(sici)1098-2795(199810)51:2<167::aid-mrd6>3.0.co;2-o;
RA Hoyer-Fender S., Petersen C., Brohmann H., Rhee K., Wolgemuth D.J.;
RT "Mouse Odf2 cDNAs consist of evolutionary conserved as well as highly
RT variable sequences and encode outer dense fiber proteins of the sperm
RT tail.";
RL Mol. Reprod. Dev. 51:167-175(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Spleen;
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] (ISOFORM 3).
RC STRAIN=C57BL/6J; 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 [5]
RP TISSUE SPECIFICITY, AND INTERACTION WITH ODF1.
RX PubMed=9045620; DOI=10.1074/jbc.272.10.6105;
RA Shao X., Tarnasky H.A., Schalles U., Oko R., van der Hoorn F.A.;
RT "Interactional cloning of the 84-kDa major outer dense fiber protein Odf84.
RT Leucine zippers mediate associations of Odf84 and Odf27.";
RL J. Biol. Chem. 272:6105-6113(1997).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=15852003; DOI=10.1038/ncb1251;
RA Ishikawa H., Kubo A., Tsukita S., Tsukita S.;
RT "Odf2-deficient mother centrioles lack distal/subdistal appendages and the
RT ability to generate primary cilia.";
RL Nat. Cell Biol. 7:517-524(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=23386061; DOI=10.1038/emboj.2013.3;
RA Kodani A., Salome Sirerol-Piquer M., Seol A., Garcia-Verdugo J.M.,
RA Reiter J.F.;
RT "Kif3a interacts with Dynactin subunit p150 Glued to organize centriole
RT subdistal appendages.";
RL EMBO J. 32:597-607(2013).
RN [9] {ECO:0000305}
RP INTERACTION WITH TSSK4.
RX PubMed=25361759; DOI=10.1093/molehr/gau097;
RA Wang X., Wei Y., Fu G., Li H., Saiyin H., Lin G., Wang Z., Chen S., Yu L.;
RT "Tssk4 is essential for maintaining the structural integrity of sperm
RT flagellum.";
RL Mol. Hum. Reprod. 21:136-145(2015).
RN [10]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=27682589; DOI=10.1091/mbc.e16-05-0318;
RA Zhang Z., Li W., Zhang Y., Zhang L., Teves M.E., Liu H., Strauss J.F. III,
RA Pazour G.J., Foster J.A., Hess R.A., Zhang Z.;
RT "Intraflagellar transport protein IFT20 is essential for male fertility and
RT spermiogenesis in mice.";
RL Mol. Biol. Cell 0:0-0(2016).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH TSSK4, AND
RP PHOSPHORYLATION AT SER-95.
RX PubMed=26961893; DOI=10.1038/srep22861;
RA Wang X., Li H., Fu G., Wang Y., Du S., Yu L., Wei Y., Chen S.;
RT "Testis-specific serine/threonine protein kinase 4 (Tssk4) phosphorylates
RT Odf2 at Ser-76.";
RL Sci. Rep. 6:22861-22861(2016).
RN [12]
RP INTERACTION WITH AKNA.
RX PubMed=30787442; DOI=10.1038/s41586-019-0962-4;
RA Camargo Ortega G., Falk S., Johansson P.A., Peyre E., Broix L., Sahu S.K.,
RA Hirst W., Schlichthaerle T., De Juan Romero C., Draganova K., Vinopal S.,
RA Chinnappa K., Gavranovic A., Karakaya T., Steininger T., Merl-Pham J.,
RA Feederle R., Shao W., Shi S.H., Hauck S.M., Jungmann R., Bradke F.,
RA Borrell V., Geerlof A., Reber S., Tiwari V.K., Huttner W.B.,
RA Wilsch-Braeuninger M., Nguyen L., Goetz M.;
RT "The centrosome protein AKNA regulates neurogenesis via microtubule
RT organization.";
RL Nature 567:113-117(2019).
RN [13]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH CFAP58.
RX PubMed=31904090; DOI=10.1042/bsr20192666;
RA Li Z.Z., Zhao W.L., Wang G.S., Gu N.H., Sun F.;
RT "The novel testicular enrichment protein Cfap58 is required for Notch-
RT associated ciliogenesis.";
RL Biosci. Rep. 40:0-0(2020).
CC -!- FUNCTION: Seems to be a major component of sperm tail outer dense
CC fibers (ODF). ODFs are filamentous structures located on the outside of
CC the axoneme in the midpiece and principal piece of the mammalian sperm
CC tail and may help to maintain the passive elastic structures and
CC elastic recoil of the sperm tail. May have a modulating influence on
CC sperm motility. Functions as a general scaffold protein that is
CC specifically localized at the distal/subdistal appendages of mother
CC centrioles. Component of the centrosome matrix required for the
CC localization of PLK1 and NIN to the centrosomes. Required for the
CC formation and/or maintenance of normal CETN1 assembly (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:15852003}.
CC -!- SUBUNIT: Self-associates. Associates with microtubules and forms a
CC fibrillar structure partially linked to the microtubule network.
CC Interacts via its C-terminus with PLK1 (By similarity). Interacts with
CC ODF1 (PubMed:9045620). Interacts with MARK4; the interaction is
CC required for localization of ODF2 to centrioles (By similarity).
CC Interacts with TSSK4 (PubMed:25361759, PubMed:26961893). Interacts with
CC AKNA (PubMed:30787442). Interacts with CFAP58 (PubMed:31904090).
CC {ECO:0000250|UniProtKB:Q5BJF6, ECO:0000269|PubMed:25361759,
CC ECO:0000269|PubMed:26961893, ECO:0000269|PubMed:30787442,
CC ECO:0000269|PubMed:31904090, ECO:0000269|PubMed:9045620}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:15852003,
CC ECO:0000269|PubMed:23386061, ECO:0000269|PubMed:31904090}. Cell
CC projection, cilium {ECO:0000269|PubMed:15852003}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:15852003}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:15852003}. Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:27682589, ECO:0000269|PubMed:31904090}.
CC Note=Localized at the microtubule organizing centers in interphase and
CC spindle poles in mitosis. Localized at the distal/subdistal appendages
CC of mother centrioles. {ECO:0000269|PubMed:15852003}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=A3KGV1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A3KGV1-2; Sequence=VSP_027672, VSP_027673;
CC Name=3;
CC IsoId=A3KGV1-3; Sequence=VSP_027672;
CC Name=4;
CC IsoId=A3KGV1-4; Sequence=VSP_027672, VSP_027674;
CC Name=5;
CC IsoId=A3KGV1-5; Sequence=VSP_027672, VSP_027675, VSP_027676;
CC Name=6; Synonyms=ODF2/2;
CC IsoId=A3KGV1-6; Sequence=VSP_027673, VSP_027675, VSP_027676;
CC Name=7; Synonyms=ODF2/1;
CC IsoId=A3KGV1-7; Sequence=VSP_027671, VSP_027675, VSP_027676;
CC -!- TISSUE SPECIFICITY: Testis-specific (at protein level) (PubMed:9045620,
CC PubMed:27682589, PubMed:31904090). Expressed in spermatids at tubular
CC stage V of the spermatogenic cycle (PubMed:9740324). Highly expressed
CC in the cytoplasm of elongating spermatids (tubular stages X/XI)
CC (PubMed:9740324). In step 14/15 spermatids of tubular stage III/IV low
CC expression detected (PubMed:9740324). No expression detected in other
CC testicular cells as well as the early round of spermatids
CC (PubMed:9740324). {ECO:0000269|PubMed:27682589,
CC ECO:0000269|PubMed:31904090, ECO:0000269|PubMed:9045620,
CC ECO:0000269|PubMed:9740324}.
CC -!- PTM: Tyrosine phosphorylated (By similarity). Phosphorylated on Ser-95
CC by TSSK4 (PubMed:26961893). {ECO:0000250|UniProtKB:Q2MJU7,
CC ECO:0000269|PubMed:26961893}.
CC -!- DISRUPTION PHENOTYPE: Null mutations in F9 embryonic carcinoma cells
CC eliminated distal/subdistal appendages and prevented primary cilium
CC formation. Loss of ODF2 also disrupted two mother centriole-specific
CC NIN dots, while leaving one dot on the proximal end of mother and
CC daughter centrioles. {ECO:0000269|PubMed:15852003}.
CC -!- SIMILARITY: Belongs to the ODF2 family. {ECO:0000305}.
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DR EMBL; AF000968; AAB65157.1; -; mRNA.
DR EMBL; AF034105; AAB87525.1; -; mRNA.
DR EMBL; AK143726; BAE25517.1; -; mRNA.
DR EMBL; AK168415; BAE40330.1; -; mRNA.
DR EMBL; AL928926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057001; AAH57001.1; -; mRNA.
DR CCDS; CCDS15861.1; -. [A3KGV1-6]
DR CCDS; CCDS50555.1; -. [A3KGV1-4]
DR CCDS; CCDS50556.1; -. [A3KGV1-3]
DR CCDS; CCDS50557.1; -. [A3KGV1-5]
DR CCDS; CCDS89461.1; -. [A3KGV1-1]
DR CCDS; CCDS89462.1; -. [A3KGV1-2]
DR PIR; T02298; T02298.
DR PIR; T09400; T09400.
DR RefSeq; NP_001106684.1; NM_001113213.1. [A3KGV1-3]
DR RefSeq; NP_001106685.1; NM_001113214.1. [A3KGV1-5]
DR RefSeq; NP_001171130.1; NM_001177659.1. [A3KGV1-4]
DR RefSeq; NP_001171132.1; NM_001177661.1.
DR RefSeq; NP_038643.1; NM_013615.3. [A3KGV1-6]
DR RefSeq; XP_017171778.1; XM_017316289.1.
DR RefSeq; XP_017171779.1; XM_017316290.1. [A3KGV1-4]
DR RefSeq; XP_017171780.1; XM_017316291.1. [A3KGV1-4]
DR RefSeq; XP_017171781.1; XM_017316292.1. [A3KGV1-4]
DR RefSeq; XP_017171782.1; XM_017316293.1. [A3KGV1-3]
DR RefSeq; XP_017171793.1; XM_017316304.1. [A3KGV1-2]
DR RefSeq; XP_017171794.1; XM_017316305.1.
DR AlphaFoldDB; A3KGV1; -.
DR SMR; A3KGV1; -.
DR BioGRID; 201898; 141.
DR IntAct; A3KGV1; 3.
DR STRING; 10090.ENSMUSP00000109388; -.
DR iPTMnet; A3KGV1; -.
DR PhosphoSitePlus; A3KGV1; -.
DR REPRODUCTION-2DPAGE; A3KGV1; -.
DR REPRODUCTION-2DPAGE; IPI00130958; -.
DR EPD; A3KGV1; -.
DR jPOST; A3KGV1; -.
DR MaxQB; A3KGV1; -.
DR PaxDb; A3KGV1; -.
DR PeptideAtlas; A3KGV1; -.
DR PRIDE; A3KGV1; -.
DR ProteomicsDB; 293486; -. [A3KGV1-1]
DR ProteomicsDB; 293487; -. [A3KGV1-2]
DR ProteomicsDB; 293488; -. [A3KGV1-3]
DR ProteomicsDB; 293489; -. [A3KGV1-4]
DR ProteomicsDB; 293490; -. [A3KGV1-5]
DR ProteomicsDB; 293491; -. [A3KGV1-6]
DR ProteomicsDB; 293492; -. [A3KGV1-7]
DR Antibodypedia; 976; 256 antibodies from 34 providers.
DR Ensembl; ENSMUST00000028128; ENSMUSP00000028128; ENSMUSG00000026790. [A3KGV1-6]
DR Ensembl; ENSMUST00000046571; ENSMUSP00000049272; ENSMUSG00000026790. [A3KGV1-3]
DR Ensembl; ENSMUST00000113755; ENSMUSP00000109384; ENSMUSG00000026790. [A3KGV1-5]
DR Ensembl; ENSMUST00000113756; ENSMUSP00000109385; ENSMUSG00000026790. [A3KGV1-3]
DR Ensembl; ENSMUST00000113757; ENSMUSP00000109386; ENSMUSG00000026790. [A3KGV1-2]
DR Ensembl; ENSMUST00000113759; ENSMUSP00000109388; ENSMUSG00000026790. [A3KGV1-4]
DR Ensembl; ENSMUST00000113763; ENSMUSP00000109392; ENSMUSG00000026790. [A3KGV1-6]
DR Ensembl; ENSMUST00000113764; ENSMUSP00000109393; ENSMUSG00000026790. [A3KGV1-6]
DR Ensembl; ENSMUST00000113765; ENSMUSP00000109394; ENSMUSG00000026790. [A3KGV1-1]
DR GeneID; 18286; -.
DR KEGG; mmu:18286; -.
DR UCSC; uc008jaj.2; mouse. [A3KGV1-5]
DR UCSC; uc008jak.2; mouse. [A3KGV1-3]
DR UCSC; uc008jam.2; mouse. [A3KGV1-6]
DR UCSC; uc033hmh.1; mouse. [A3KGV1-4]
DR CTD; 4957; -.
DR MGI; MGI:1098824; Odf2.
DR VEuPathDB; HostDB:ENSMUSG00000026790; -.
DR eggNOG; ENOG502QUXQ; Eukaryota.
DR GeneTree; ENSGT00530000063497; -.
DR HOGENOM; CLU_018326_0_0_1; -.
DR InParanoid; A3KGV1; -.
DR OMA; MEWRYQS; -.
DR OrthoDB; 328077at2759; -.
DR PhylomeDB; A3KGV1; -.
DR TreeFam; TF328605; -.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 18286; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Odf2; mouse.
DR PRO; PR:A3KGV1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A3KGV1; protein.
DR Bgee; ENSMUSG00000026790; Expressed in seminiferous tubule of testis and 270 other tissues.
DR ExpressionAtlas; A3KGV1; baseline and differential.
DR Genevisible; A3KGV1; MM.
DR GO; GO:0120103; C:centriolar subdistal appendage; ISO:MGI.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR GO; GO:0097539; C:ciliary transition fiber; IDA:MGI.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0001520; C:outer dense fiber; ISO:MGI.
DR GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:MGI.
DR GO; GO:0010457; P:centriole-centriole cohesion; ISO:MGI.
DR GO; GO:0044782; P:cilium organization; ISO:MGI.
DR GO; GO:0008104; P:protein localization; ISO:MGI.
DR GO; GO:1902017; P:regulation of cilium assembly; ISO:MGI.
DR GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR InterPro; IPR026099; Odf2-rel.
DR PANTHER; PTHR23162; PTHR23162; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium; Coiled coil; Cytoplasm;
KW Cytoskeleton; Developmental protein; Differentiation; Flagellum;
KW Isopeptide bond; Microtubule; Phosphoprotein; Reference proteome;
KW Spermatogenesis; Ubl conjugation.
FT CHAIN 1..830
FT /note="Outer dense fiber protein 2"
FT /id="PRO_0000299458"
FT COILED 144..217
FT /evidence="ECO:0000255"
FT COILED 245..423
FT /evidence="ECO:0000255"
FT COILED 461..798
FT /evidence="ECO:0000255"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 92
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 95
FT /note="Phosphoserine; by TSSK4"
FT /evidence="ECO:0000269|PubMed:26961893"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 110
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 231
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5BJF6"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5BJF6"
FT VAR_SEQ 1..47
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:9740324"
FT /id="VSP_027671"
FT VAR_SEQ 1..41
FT /note="MSASSSGGSPRFPSCGKNGVTSLTQKKVLRTPCGAPSVTVT -> MKDRSST
FT PPLHVHVDENTPVHVHIKKLPKPSAASSQ (in isoform 2, isoform 3,
FT isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_027672"
FT VAR_SEQ 65..83
FT /note="Missing (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:9740324"
FT /id="VSP_027673"
FT VAR_SEQ 281
FT /note="E -> EK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027674"
FT VAR_SEQ 638..657
FT /note="IEHQGDKLEMAREKHQASQK -> VRDWQKGSHELARAGARLPR (in
FT isoform 5, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9740324"
FT /id="VSP_027675"
FT VAR_SEQ 658..830
FT /note="Missing (in isoform 5, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9740324"
FT /id="VSP_027676"
FT CONFLICT 349
FT /note="L -> W (in Ref. 2; AAH57001)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 830 AA; 95541 MW; C840B47EC10EF82A CRC64;
MSASSSGGSP RFPSCGKNGV TSLTQKKVLR TPCGAPSVTV TKSHKRGMKG DTVNVRRSVR
VKTKVPWMPP GKSSARHVGC KWENPPHCLE ITPPSSEKLV SVMRLSDLST EDDDSGHCKM
NRYDKKIDSL MNAVGCLKSE VKMQKGERQM AKRFLEERKE ELEEVAHELA ETEHENTVLR
HNIERIKEEK DFTMLQKKHL QQEKECLMSK LVEAEMDGAA AAKQVMALKD TIGKLKTEKQ
MTCTDINTLT RQKELLLQKL STFEETNRTL RDLLREQHCK EDSERLMEQQ GTLLKRLAEA
DSEKARLLLL LQDKDKEVEE LLQEIQCEKA QAKTASELSK SMESMRGHLQ AQLRCKEAEN
SRLCMQIKNL ERSGNQHKAE VEAIMEQLKE LKQKGDRDKE TLKKAIRAQK ERAEKSEEYA
EQLHVQLADK DLYVAEALST LESWRSRYNQ VVKDKGDLEL EIIVLNDRVT DLVNQQQSLE
EKMREDRDSL VERLHRQTAE YSAFKLENER LKASFAPMED KLNQAHLEVQ QLKASVKNYE
GMIDNYKSQV MKTRLEADEV AAQLERCDKE NKMLKDEMNK EIEAARRQFQ SQLADLQQLP
DILKITEAKL AECQDQLQGY ERKNIDLTAI ISDLRSRIEH QGDKLEMARE KHQASQKENK
QLSQKVDELE RKLEATSAQN VEFLQVIAKR EEAIHQAQLR LEEKTRECGS LARQLESAIE
DARRQVEQTK EQALSKERAA QSKILDLETQ LSRTKTELGQ LRRTRDDADR RYQSRLQDLK
DRLEQSESTN RSMQNYVQFL KASYANVFGD APYTSSYLTS SPIRSRSPPA
