ODFP2_MACFA
ID ODFP2_MACFA Reviewed; 638 AA.
AC Q4R8C3; Q4R861;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 50.
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; ORFNames=QtsA-12846, QtsA-13326;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-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. Localized
CC at the distal/subdistal appendages of mother centrioles. Interacts with
CC MARK4; the interaction is required for localization of ODF2 to
CC centrioles. Interacts with TSSK4. Interacts with AKNA. Interacts with
CC QRICH2 (By similarity). Interacts with CFAP58 (By similarity).
CC {ECO:0000250|UniProtKB:A3KGV1, 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4R8C3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4R8C3-2; Sequence=VSP_027670;
CC -!- PTM: Tyrosine phosphorylated. Phosphorylated on Ser-76 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; AB168532; BAE00649.1; -; mRNA.
DR EMBL; AB168597; BAE00711.1; -; mRNA.
DR AlphaFoldDB; Q4R8C3; -.
DR SMR; Q4R8C3; -.
DR STRING; 9541.XP_005580788.1; -.
DR eggNOG; ENOG502QUXQ; Eukaryota.
DR Proteomes; UP000233100; 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 2: Evidence at transcript 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..638
FT /note="Outer dense fiber protein 2"
FT /id="PRO_0000299457"
FT REGION 373..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 125..198
FT /evidence="ECO:0000255"
FT COILED 226..404
FT /evidence="ECO:0000255"
FT COILED 442..616
FT /evidence="ECO:0000255"
FT MOD_RES 73
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 76
FT /note="Phosphoserine; by TSSK4"
FT /evidence="ECO:0000250|UniProtKB:A3KGV1"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 91
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 212
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5BJF6"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5BJF6"
FT VAR_SEQ 1..68
FT /note="MSASSSGGSPRFPSCGKNGVTSLTQKKVLRAPCGAPSVTVTKSHKRGMKGDT
FT VNVRRSVRVKTKNPPR -> MPPGKSSARPVGCKWENPPH (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_027670"
FT CONFLICT 231
FT /note="A -> T (in Ref. 1; BAE00711)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 638 AA; 73330 MW; 8DCD2DAC6948F79B CRC64;
MSASSSGGSP RFPSCGKNGV TSLTQKKVLR APCGAPSVTV TKSHKRGMKG DTVNVRRSVR
VKTKNPPRCL EITPPSSEKL VSVMRLSDLS TEDDDSGHCK MNRYDKKIDS LMNAVGCLKS
EVKMQKGERQ MAKRFLEERK EELEEVAHEL AETEHENTVL RHNIERMKEE KDYTILQKKH
LQQEKECLMS KLVEAEMDGA AAAKQVMALK DTIGKLKTEK QMTCTDINTL ARQKELLLQK
LSTFEETNRT LRDLLREQHC KEDSERLMEQ QGALLKRLAE ADSEKARLLL LLQDKDKEVE
ELLQEIQCEK AQAKTASELS KSMESMRGHL QAQLRSKEAE NSRLCMQIKN LERSGNQHKA
EVEAIMEQLK ELKQKGDRDK ESLKKAIRAQ KERAEKSEEY AEQLHVQLAD KDLYVAEALS
TLESWRSRYN QVVKDKGDLE LEIIVLNDRV TDLVNQQQTL EEKMREDRDS LVERLHRQTA
EYSAFKLENE RLKASFAPME DKLNQAHLEV QQLKASVKNY EGMIDNYKSQ VMKTRLEADE
VAAQLERCDK ENKILKDEMN KEIEAARRQF QSQLADLQQL PDILKITEAK LAECQDQLQG
YERKNIDLTA IISDLRSRVR DWQKGSHELT RAGARIPR
