ODFP2_BOVIN
ID ODFP2_BOVIN Reviewed; 657 AA.
AC Q2T9U2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Outer dense fiber protein 2;
DE AltName: Full=Cenexin;
DE AltName: Full=Outer dense fiber of sperm tails protein 2;
GN Name=ODF2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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. Interacts with ODF1. Interacts
CC with MARK4; the interaction is required for localization of ODF2 to
CC centrioles. Interacts with TSSK4. Interacts with AKNA (By similarity).
CC Interacts with CFAP58 (By similarity). {ECO:0000250|UniProtKB:A3KGV1,
CC ECO:0000250|UniProtKB:Q5BJF6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:A3KGV1}. Cell projection,
CC cilium {ECO:0000250|UniProtKB:A3KGV1}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:A3KGV1}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:A3KGV1}. 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 -!- PTM: Tyrosine phosphorylated. Phosphorylated on Ser-95 by TSSK4.
CC {ECO:0000250|UniProtKB:A3KGV1, ECO:0000250|UniProtKB:Q2MJU7}.
CC -!- SIMILARITY: Belongs to the ODF2 family. {ECO:0000305}.
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DR EMBL; BC111268; AAI11269.1; -; mRNA.
DR RefSeq; NP_001033269.1; NM_001038180.2.
DR AlphaFoldDB; Q2T9U2; -.
DR SMR; Q2T9U2; -.
DR STRING; 9913.ENSBTAP00000020325; -.
DR PaxDb; Q2T9U2; -.
DR PRIDE; Q2T9U2; -.
DR GeneID; 539043; -.
DR KEGG; bta:539043; -.
DR CTD; 4957; -.
DR eggNOG; ENOG502QUXQ; Eukaryota.
DR InParanoid; Q2T9U2; -.
DR OrthoDB; 328077at2759; -.
DR Proteomes; UP000009136; 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:1902017; P:regulation of cilium assembly; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR026099; Odf2-rel.
DR PANTHER; PTHR23162; PTHR23162; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; Flagellum; Isopeptide bond;
KW Microtubule; Phosphoprotein; Reference proteome; Spermatogenesis;
KW Ubl conjugation.
FT CHAIN 1..657
FT /note="Outer dense fiber protein 2"
FT /id="PRO_0000299456"
FT COILED 144..423
FT /evidence="ECO:0000255"
FT COILED 461..635
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:0000250|UniProtKB:A3KGV1"
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"
SQ SEQUENCE 657 AA; 75498 MW; E63F67E536094D9E CRC64;
MSASSSGGSP RFPSCGKNGV TSLTQKKVLR TPCGAPSVTV TKSHKRGMKG DTVNVRRSVR
VKTKVPWMPP GKSSARHVGC NWENPPHCLE ITPPSSEKLV SVMRLSDLST EDDDSGHCKM
NRYDKKIDSL MNAVGCLKSE VKMQKGERQM AKRFLEERKE ELEEVAQELA ETEHENTVLR
HNIERIKEEK DYTMLQKKHL QQEKECLMSK LVEAEMDGAA AAKQVMALKD TIGKLKSEKQ
MTCSDINTLT RQKELLLQKL STFEETNRTL RDLLREQHCK EDSERLMEQQ GTLLKRLAEA
DSEKARLLLL LQDKDKEVEE LLQEIQCEKA QAKTASELSK SMETMRGHLQ AQLRCKEAEN
SRLCMQIKNL ERSGNQHKAE VEAIMEQLKE LKQKGERDKE SLKKAIRAQK ERAEKSEEYA
EQLHVQLADK DLYVAEALST LESWRSRYNQ VVKDKGDLEL EIIVLNDRVT DLVNQQQTLE
EKMREDRDSL VERLHRQTAE YSAFKLENER LKASFAPMED KLNQAHIEVQ QLKASVKNYE
GMIDNYKSQV MKTRLEADEV AAQLERCDKE NKILKDEMNK EIEAARRQFQ SQLADLQQLP
DILKITEAKL AECQDQLQGY ERKNIDLTAI ISDLRSRVRD WQKGSHELAR AGARLPR
