ID   ODFP2_PONAB             Reviewed;         680 AA.
AC   Q5R829;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 63.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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. 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   -!- PTM: Tyrosine phosphorylated. Phosphorylated on Ser-90 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; CR859926; CAH92081.1; -; mRNA.
DR   RefSeq; NP_001126214.1; NM_001132742.1.
DR   AlphaFoldDB; Q5R829; -.
DR   SMR; Q5R829; -.
DR   STRING; 9601.ENSPPYP00000022026; -.
DR   GeneID; 100173182; -.
DR   KEGG; pon:100173182; -.
DR   CTD; 4957; -.
DR   eggNOG; ENOG502QUXQ; Eukaryota.
DR   InParanoid; Q5R829; -.
DR   OrthoDB; 328077at2759; -.
DR   Proteomes; UP000001595; 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   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..680
FT                   /note="Outer dense fiber protein 2"
FT                   /id="PRO_0000299459"
FT   REGION          27..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          387..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          632..680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          139..212
FT                   /evidence="ECO:0000255"
FT   COILED          275..418
FT                   /evidence="ECO:0000255"
FT   COILED          456..630
FT                   /evidence="ECO:0000255"
FT   MOD_RES         68
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT   MOD_RES         69
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT   MOD_RES         87
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT   MOD_RES         90
FT                   /note="Phosphoserine; by TSSK4"
FT                   /evidence="ECO:0000250|UniProtKB:A3KGV1"
FT   MOD_RES         101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT   MOD_RES         104
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT   MOD_RES         105
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT   MOD_RES         110
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT   MOD_RES         124
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT   MOD_RES         134
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT   MOD_RES         226
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5BJF6"
FT   MOD_RES         256
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT   MOD_RES         627
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT   CROSSLNK        133
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q5BJF6"
SQ   SEQUENCE   680 AA;  77941 MW;  E1F6D0079019676B CRC64;
     MKDRSSTPPL HVHVDENTPV HVHIKKLPKP SATSSQKSHK RGMKGDTVNV RRSVRVKTKV
     PWMPPGKSSA RPVGCKWENP PHCLEITPPS SEKLVSVMRL SDLSTEDDDS GHCKMNRYDK
     KIDSLMNAVG CLKSEVKMQK GERQMAKRFL EERKEELEEV AHELAETEHE NTVLRHNIER
     MKEEKDFTIL QKKHLQQEKE CLMSKLVEAE MDGAAAAKQV MALKDTIGKL KTEKQMTCTD
     INTLTRQKEL LLQKLSTFGE TNRTLRDLLR EQHCKEDSER LMEQQGALLK RLAEADSEKA
     RLLLLLRDKD KEVEELLQEI QCEKAQAKTA SELSKSMESM RGHLQAQLRS KEAENSRLCM
     QIKNLERSGN QHKAEVEAIM EQLKELKQKG DRDKESLKKA IRAQKERAEK SEEYAEQLHV
     QLADKDLYVA EALSTLESWR SRYNQVVKDK GDLELEIIVL NDRVTDLVNQ QQTLEEKMRE
     DRDSLVERLH RQTAEYSAFK LENERLKASF APMEDKLNQA HLEVQQLKAS VKNYEGMIDN
     YKSQVMKTRL EADEVAAQLE RCDKENKILK DEMNKEIEAA RRQFQSQLAD LQQLPDILKI
     TEAKLAECQD QLQGYERKNI DLTAIISDLR SRETGGDQCP EYRVPTGDCQ EGGGNPPVPA
     AARGENTGMW DPGKAVGERH