ODFP2_MESAU
ID ODFP2_MESAU Reviewed; 124 AA.
AC Q2MJU7; P86236; P86266;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Outer dense fiber protein 2 {ECO:0000250|UniProtKB:Q6AYX5, ECO:0000312|EMBL:ABC49850.1};
DE AltName: Full=84 kDa outer dense fiber protein {ECO:0000250|UniProtKB:Q6AYX5};
DE AltName: Full=Cenexin {ECO:0000250|UniProtKB:Q6AYX5};
DE AltName: Full=Outer dense fiber of sperm tails protein 2 {ECO:0000250|UniProtKB:Q6AYX5};
DE Flags: Fragment;
GN Name=ODF2 {ECO:0000250|UniProtKB:Q6AYX5};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABC49850.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, PHOSPHORYLATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Testis {ECO:0000269|PubMed:19953638};
RX PubMed=19953638; DOI=10.1002/mrd.21131;
RA Mariappa D., Aladakatti R.H., Dasari S.K., Sreekumar A., Wolkowicz M.,
RA van der Hoorn F., Seshagiri P.B.;
RT "Inhibition of tyrosine phosphorylation of sperm flagellar proteins, outer
RT dense fiber protein-2 and tektin-2, is associated with impaired motility
RT during capacitation of hamster spermatozoa.";
RL Mol. Reprod. Dev. 77:182-193(2010).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
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|UniProtKB:Q6AYX5}.
CC -!- SUBUNIT: Self-associates. Associates with microtubules and forms a
CC fibrillar structure partially linked to the microtubule network.
CC Interacts through its C-terminus with PLK1. Interacts with ODF1.
CC Interacts with MARK4; the interaction is required for localization of
CC ODF2 to centrioles. Interacts with TSSK4. Interacts with AKNA.
CC Interacts with QRICH2 (By similarity). Interacts with CFAP58 (By
CC similarity). {ECO:0000250|UniProtKB:A3KGV1,
CC ECO:0000250|UniProtKB:Q5BJF6, ECO:0000250|UniProtKB:Q6AYX5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q6AYX5}. Cell projection,
CC cilium {ECO:0000250|UniProtKB:Q6AYX5}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q6AYX5}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q6AYX5}. Cell projection, cilium, flagellum
CC {ECO:0000250|UniProtKB:A3KGV1}. Note=Localized at the microtubule
CC organizing centers in interphase and spindle poles in mitosis.
CC Localized at the distal/subdistal appendages of mother centrioles.
CC {ECO:0000250|UniProtKB:A3KGV1}.
CC -!- TISSUE SPECIFICITY: Detected in sperm flagella (at protein level).
CC {ECO:0000269|PubMed:19953638}.
CC -!- PTM: Tyrosine phosphorylated. {ECO:0000269|PubMed:19953638}.
CC -!- SIMILARITY: Belongs to the ODF2 family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ322652; ABC49850.1; -; mRNA.
DR AlphaFoldDB; Q2MJU7; -.
DR SMR; Q2MJU7; -.
DR STRING; 10036.XP_005139333.1; -.
DR eggNOG; ENOG502QUXQ; Eukaryota.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR026099; Odf2-rel.
DR PANTHER; PTHR23162; PTHR23162; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; Flagellum; Microtubule;
KW Phosphoprotein; Reference proteome; Spermatogenesis.
FT CHAIN <1..>124
FT /note="Outer dense fiber protein 2"
FT /id="PRO_0000394747"
FT COILED 13..124
FT /evidence="ECO:0000255"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:ABC49850.1"
FT NON_TER 124
FT /evidence="ECO:0000312|EMBL:ABC49850.1"
SQ SEQUENCE 124 AA; 14385 MW; AEFDFCE98398C342 CRC64;
RTLRDLLREQ HSKEDSERLM EQQGALLKRL AEADSEKARL LLLLQDKDKE VEELLQEIQC
EKAQAKTASE LSKSMESMRG HLQAQLRCKE AENSRLCMQI KNLERSGNQH KAEVEAIMEQ
LKEL
