ROP1_MOUSE
ID ROP1_MOUSE Reviewed; 212 AA.
AC Q9ESG2; Q3TVG5;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Ropporin-1;
DE AltName: Full=Rhophilin-associated 'oppo' protein;
DE AltName: Full=Rhophilin-associated protein 1;
GN Name=Ropn1;
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], SUBUNIT, INTERACTION WITH RHPN1, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=10591629; DOI=10.1242/jcs.113.1.103;
RA Fujita A., Nakamura K., Kato T., Watanabe N., Ishizaki T., Kimura K.,
RA Mizoguchi A., Narumiya S.;
RT "Ropporin, a sperm-specific binding protein of rhophilin, that is localized
RT in the fibrous sheath of sperm flagella.";
RL J. Cell Sci. 113:103-112(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 62-212.
RC STRAIN=C57BL/6J; TISSUE=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 [4]
RP SUBCELLULAR LOCATION.
RX PubMed=11278869; DOI=10.1074/jbc.m011252200;
RA Carr D.W., Fujita A., Stentz C.L., Liberty G.A., Olson G.E., Narumiya S.;
RT "Identification of sperm-specific proteins that interact with A-kinase
RT anchoring proteins in a manner similar to the type II regulatory subunit of
RT PKA.";
RL J. Biol. Chem. 276:17332-17338(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=23303679; DOI=10.1095/biolreprod.112.105262;
RA Fiedler S.E., Dudiki T., Vijayaraghavan S., Carr D.W.;
RT "Loss of R2D2 proteins ROPN1 and ROPN1L causes defects in murine sperm
RT motility, phosphorylation, and fibrous sheath integrity.";
RL Biol. Reprod. 88:41-41(2013).
RN [7]
RP SUMOYLATION, AND INTERACTION WITH FSCB.
RX PubMed=27398160;
RA Zhang X., Chen M., Yu R., Liu B., Tian Z., Liu S.;
RT "FSCB phosphorylation regulates mouse spermatozoa capacitation through
RT suppressing SUMOylation of ROPN1/ROPN1L.";
RL Am. J. Transl. Res. 8:2776-2782(2016).
CC -!- FUNCTION: Important for male fertility. With ROPN1L, involved in
CC fibrous sheath integrity and sperm motility, plays a role in PKA-
CC dependent signaling processes required for spermatozoa capacitation.
CC {ECO:0000269|PubMed:23303679}.
CC -!- SUBUNIT: Homodimer. Interacts with AKAP3 (By similarity). May interact
CC with SPA17 (By similarity). Interacts with RHPN1 (PubMed:10591629).
CC Interacts with FSCB; the interaction increases upon spermatozoa
CC capacitation conditions (PubMed:27398160).
CC {ECO:0000250|UniProtKB:Q96C74, ECO:0000250|UniProtKB:Q9BZX4,
CC ECO:0000269|PubMed:10591629, ECO:0000269|PubMed:27398160}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:11278869, ECO:0000269|PubMed:23303679}. Note=In the
CC sperm tail, found in the principal piece and in the cytoplasmic droplet
CC located at the distal end of the midpiece. Inner surface of the fibrous
CC sheath.
CC -!- TISSUE SPECIFICITY: Testis-specific. Present in the most inner parts of
CC seminiferous tubules (at protein level). {ECO:0000269|PubMed:10591629,
CC ECO:0000269|PubMed:23303679}.
CC -!- DEVELOPMENTAL STAGE: Expression in testis starts at P21, and increases
CC to reach a plateau at P27 (PubMed:10591629). Expressed in the flagella
CC of sperm at all stages of development in the testis and epididymis
CC (PubMed:23303679). {ECO:0000269|PubMed:10591629,
CC ECO:0000269|PubMed:23303679}.
CC -!- DOMAIN: The RIIa domain mediates interaction with AKAP3. {ECO:0000250}.
CC -!- PTM: Sumoylated, sumoylation decreases upon spermatozoa capacitation
CC conditions. {ECO:0000269|PubMed:27398160}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are subfertile with normal testicular
CC morphology and spermatogenesis but moderately impaired motility and
CC increased levels of ROPN1L (PubMed:23303679). Double knockout animals
CC for ROPN1 and ROPN1L are infertile with normal testicular morphology
CC and spermatogenesis but defects in sperm morphology, thinning and
CC shredding of the principal piece. Sperm is immotile (PubMed:23303679).
CC {ECO:0000269|PubMed:23303679}.
CC -!- MISCELLANEOUS: 'Ropporin' comes from the Japanese word 'oppo' which
CC means 'tail'.
CC -!- SIMILARITY: Belongs to the ropporin family. {ECO:0000305}.
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DR EMBL; AF178531; AAG09309.1; -; mRNA.
DR EMBL; BC049544; AAH49544.1; -; mRNA.
DR EMBL; AK160142; BAE35653.1; -; mRNA.
DR CCDS; CCDS28137.1; -.
DR RefSeq; NP_109669.1; NM_030744.2.
DR RefSeq; XP_006522761.1; XM_006522698.3.
DR AlphaFoldDB; Q9ESG2; -.
DR CORUM; Q9ESG2; -.
DR IntAct; Q9ESG2; 3.
DR MINT; Q9ESG2; -.
DR STRING; 10090.ENSMUSP00000023530; -.
DR iPTMnet; Q9ESG2; -.
DR PhosphoSitePlus; Q9ESG2; -.
DR PaxDb; Q9ESG2; -.
DR PRIDE; Q9ESG2; -.
DR ProteomicsDB; 262698; -.
DR DNASU; 76378; -.
DR Ensembl; ENSMUST00000023530; ENSMUSP00000023530; ENSMUSG00000022832.
DR GeneID; 76378; -.
DR KEGG; mmu:76378; -.
DR UCSC; uc007zaz.1; mouse.
DR CTD; 54763; -.
DR MGI; MGI:1923628; Ropn1.
DR VEuPathDB; HostDB:ENSMUSG00000022832; -.
DR eggNOG; ENOG502R2JI; Eukaryota.
DR GeneTree; ENSGT00390000012731; -.
DR HOGENOM; CLU_069829_1_0_1; -.
DR InParanoid; Q9ESG2; -.
DR OMA; QWASDYF; -.
DR OrthoDB; 1316863at2759; -.
DR PhylomeDB; Q9ESG2; -.
DR TreeFam; TF105421; -.
DR BioGRID-ORCS; 76378; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Ropn1; mouse.
DR PRO; PR:Q9ESG2; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9ESG2; protein.
DR Bgee; ENSMUSG00000022832; Expressed in spermatid and 12 other tissues.
DR ExpressionAtlas; Q9ESG2; baseline and differential.
DR Genevisible; Q9ESG2; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031514; C:motile cilium; ISO:MGI.
DR GO; GO:0097598; C:sperm cytoplasmic droplet; IDA:MGI.
DR GO; GO:0097228; C:sperm principal piece; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0044782; P:cilium organization; IGI:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR GO; GO:0061512; P:protein localization to cilium; IGI:MGI.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:MGI.
DR GO; GO:0048240; P:sperm capacitation; IMP:MGI.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Flagellum; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..212
FT /note="Ropporin-1"
FT /id="PRO_0000307395"
FT DOMAIN 12..43
FT /note="RIIa"
FT REGION 209..212
FT /note="Interaction with RHPN1"
FT /evidence="ECO:0000269|PubMed:10591629"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4KLL5"
SQ SEQUENCE 212 AA; 24003 MW; 782EA4C6890BC50C CRC64;
MPQTDKQVCI PPELPELLKQ FTKDAIRTQP PDLIQWAAEY FGAMSRGEIP PVRERSEQIP
LSNWAELTPE LLKVLHSRVA GRLIIHADEL AQMWKVLNLP TDLFNSVMNV GRFTEEIEWL
KFLALACSSL GVTIAKTLKI VCEVLSSDHD GGPPRIPFST FQFLYTYIAE VDGEISSSHV
SRMLNYIEQE VIGPDGLIKV NDFTQNPRVR LE
