ODFP1_RAT
ID ODFP1_RAT Reviewed; 245 AA.
AC P21769; Q62652; Q63390; Q63534; Q63535;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Outer dense fiber protein 1;
DE AltName: Full=Protein RT7;
DE AltName: Full=RTS 5/1;
GN Name=Odf1; Synonyms=Odf27, Odfp, Rt7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=1936558; DOI=10.1016/0012-1606(91)90329-2;
RA Burfeind P., Hoyer-Fender S.;
RT "Sequence and developmental expression of a mRNA encoding a putative
RT protein of rat sperm outer dense fibers.";
RL Dev. Biol. 148:195-204(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Wistar; TISSUE=Spleen, and Testis;
RX PubMed=8375388; DOI=10.1111/j.1432-1033.1993.tb18168.x;
RA Burfeind P., Belgardt B., Szpirer C., Hoyer-Fender S.;
RT "Structure and chromosomal assignment of a gene encoding the major protein
RT of rat sperm outer dense fibres.";
RL Eur. J. Biochem. 216:497-505(1993).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 81-245, AND PROTEIN SEQUENCE OF 50-52 AND
RP 156-165.
RC TISSUE=Testis;
RX PubMed=8179907; DOI=10.1002/mrd.1080370215;
RA Morales C.R., Oko R., Clermont Y.;
RT "Molecular cloning and developmental expression of an mRNA encoding the 27
RT kDa outer dense fiber protein of rat spermatozoa.";
RL Mol. Reprod. Dev. 37:229-240(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-90.
RC TISSUE=Testis;
RX PubMed=1699827; DOI=10.1016/0012-1606(90)90158-f;
RA van der Hoorn F.A., Tarnasky H.A., Nordeen S.K.;
RT "A new rat gene RT7 is specifically expressed during spermatogenesis.";
RL Dev. Biol. 142:147-154(1990).
RN [6]
RP INTERACTION WITH SPAG4.
RX PubMed=10373309; DOI=10.1006/dbio.1999.9297;
RA Shao X., Tarnasky H.A., Lee J.P., Oko R., van der Hoorn F.A.;
RT "Spag4, a novel sperm protein, binds outer dense-fiber protein Odf1 and
RT localizes to microtubules of manchette and axoneme.";
RL Dev. Biol. 211:109-123(1999).
RN [7]
RP INTERACTION WITH KLC3.
RX PubMed=12594206; DOI=10.1074/jbc.m213126200;
RA Bhullar B., Zhang Y., Junco A., Oko R., van der Hoorn F.A.;
RT "Association of kinesin light chain with outer dense fibers in a
RT microtubule-independent fashion.";
RL J. Biol. Chem. 278:16159-16168(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-10; SER-64; SER-87;
RP SER-108; SER-109; SER-137; SER-153; SER-175 AND SER-180, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Component of the outer dense fibers (ODF) of spermatozoa. ODF
CC are filamentous structures located on the outside of the axoneme in the
CC midpiece and principal piece of the mammalian sperm tail and may help
CC to maintain the passive elastic structures and elastic recoil of the
CC sperm tail.
CC -!- SUBUNIT: Interacts (via leucine zipper motif) with TCP11 (By
CC similarity). Interacts with SPAG4 (PubMed:10373309). Interacts with
CC KLC3 (PubMed:12594206). {ECO:0000250|UniProtKB:Q14990,
CC ECO:0000269|PubMed:10373309, ECO:0000269|PubMed:12594206}.
CC -!- TISSUE SPECIFICITY: Testis. Specifically located to the round spermatid
CC layer and to the luminally-oriented cytoplasm of elongated spermatids.
CC -!- DEVELOPMENTAL STAGE: First detected in 30-day old rats after which,
CC levels increase during spermatid elongation. Levels decrease at the
CC time of spermatid assembly and disappear just before spermiation.
CC -!- DOMAIN: The C-terminal contains many C-X-P repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA42091.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M88759; AAA03066.1; -; mRNA.
DR EMBL; M88762; AAA42091.1; ALT_INIT; Genomic_DNA.
DR EMBL; M88762; AAA42092.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC078708; AAH78708.1; -; mRNA.
DR EMBL; U09021; AAA67872.1; -; mRNA.
DR EMBL; M58677; AAA42086.1; -; mRNA.
DR PIR; A43905; A43905.
DR RefSeq; NP_077040.2; NM_024126.5.
DR AlphaFoldDB; P21769; -.
DR SMR; P21769; -.
DR STRING; 10116.ENSRNOP00000008700; -.
DR iPTMnet; P21769; -.
DR PhosphoSitePlus; P21769; -.
DR PaxDb; P21769; -.
DR PRIDE; P21769; -.
DR GeneID; 24610; -.
DR KEGG; rno:24610; -.
DR UCSC; RGD:3228; rat.
DR CTD; 4956; -.
DR RGD; 3228; Odf1.
DR VEuPathDB; HostDB:ENSRNOG00000006578; -.
DR eggNOG; ENOG502S68A; Eukaryota.
DR HOGENOM; CLU_076121_0_0_1; -.
DR InParanoid; P21769; -.
DR OMA; LYYPCCL; -.
DR OrthoDB; 1320934at2759; -.
DR PhylomeDB; P21769; -.
DR TreeFam; TF337986; -.
DR PRO; PR:P21769; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000006578; Expressed in testis and 8 other tissues.
DR Genevisible; P21769; RN.
DR GO; GO:0001520; C:outer dense fiber; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR CDD; cd06482; ACD_HspB10; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR037552; ODF1_ACD.
DR InterPro; IPR037389; ODFP.
DR PANTHER; PTHR17125; PTHR17125; 1.
DR Pfam; PF00011; HSP20; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Phosphoprotein; Reference proteome; Repeat; Spermatogenesis.
FT CHAIN 1..245
FT /note="Outer dense fiber protein 1"
FT /id="PRO_0000058027"
FT REPEAT 34..38
FT /note="1"
FT REPEAT 74..78
FT /note="2"
FT REGION 34..78
FT /note="2 X 5 AA repeats of [RC]-C-L-C-D"
FT REGION 195..233
FT /note="C-X-P repeat region"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 88..90
FT /note="LRS -> SAA (in Ref. 5; AAA42086)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 27351 MW; 3111C776213A7381 CRC64;
MAALSCLLDS VRRDIKKVDR ELRQLRCIDE ISSRCLCDLY MHPYCCCDLH PYPYCLCYSK
RSRSCGLCDL YYPCCLCDYK LYCLRPSLRS LERLRRTTNR ILASSCCSSN ILGSVNVCGF
EPDQVKVRVK DGKVCVSAER ENRYDCLGSK KYSYMNICKE FSLPPCVDEK DVTYSYGLGS
CVKIESPCYP CTSPCNPCNP CSPCSPCGPC GPCGPCGPCG PCGPCDPCNP CYPCGSRFSC
RKMIL
