ID   PMFBP_RAT               Reviewed;         971 AA.
AC   Q9Z221;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Polyamine-modulated factor 1-binding protein 1;
DE            Short=PMF-1-binding protein;
DE   AltName: Full=Outer dense fiber protein 3;
GN   Name=Pmfbp1; Synonyms=Odf3;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=11774381; DOI=10.1002/mrd.1136;
RA   Petersen C., Aumuller G., Bahrami M., Hoyer-Fender S.;
RT   "Molecular cloning of Odf3 encoding a novel coiled-coil protein of sperm
RT   tail outer dense fibers.";
RL   Mol. Reprod. Dev. 61:102-112(2002).
CC   -!- FUNCTION: Required for normal spermatogenesis. It functions as a
CC       scaffold protein that attaches the sperm head-tail connecting piece to
CC       the nuclear envelope, thus maintaining sperm head and tail integrity.
CC       May also be involved in the general organization of cellular
CC       cytoskeleton. {ECO:0000250|UniProtKB:Q9WVQ0,
CC       ECO:0000269|PubMed:11774381}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC       {ECO:0000250|UniProtKB:Q9WVQ0}. Note=Localized at the sperm head-tail
CC       connecting piece. During spermatogenesis, it is first observed in the
CC       cytoplasm of round spermatids, it later appears in the implantation
CC       fossa region of the sperm nucleus during sperm head elongation and
CC       differentiation, and finally it localizes to the head-tail connecting
CC       piece. {ECO:0000250|UniProtKB:Q9WVQ0}.
CC   -!- TISSUE SPECIFICITY: Expressed in testis and more specifically in ODF,
CC       the sperm tail specific cytoskeletal structure. Also expressed in
CC       epididymides and brain. {ECO:0000269|PubMed:11774381}.
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DR   EMBL; AF092090; AAC72233.2; -; mRNA.
DR   RefSeq; NP_599220.1; NM_134393.2.
DR   AlphaFoldDB; Q9Z221; -.
DR   SMR; Q9Z221; -.
DR   STRING; 10116.ENSRNOP00000019577; -.
DR   iPTMnet; Q9Z221; -.
DR   PhosphoSitePlus; Q9Z221; -.
DR   PaxDb; Q9Z221; -.
DR   GeneID; 171414; -.
DR   KEGG; rno:171414; -.
DR   UCSC; RGD:621677; rat.
DR   CTD; 83449; -.
DR   RGD; 621677; Pmfbp1.
DR   eggNOG; ENOG502QUDT; Eukaryota.
DR   InParanoid; Q9Z221; -.
DR   OrthoDB; 291625at2759; -.
DR   PRO; PR:Q9Z221; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0001520; C:outer dense fiber; TAS:RGD.
DR   GO; GO:0097224; C:sperm connecting piece; ISS:UniProtKB.
DR   GO; GO:0007010; P:cytoskeleton organization; NAS:RGD.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   InterPro; IPR037391; PMF1-bd.
DR   PANTHER; PTHR18881; PTHR18881; 1.
PE   2: Evidence at transcript level;
KW   Cell projection; Cilium; Coiled coil; Flagellum; Reference proteome.
FT   CHAIN           1..971
FT                   /note="Polyamine-modulated factor 1-binding protein 1"
FT                   /id="PRO_0000304621"
FT   COILED          37..69
FT                   /evidence="ECO:0000255"
FT   COILED          117..229
FT                   /evidence="ECO:0000255"
FT   COILED          282..325
FT                   /evidence="ECO:0000255"
FT   COILED          355..680
FT                   /evidence="ECO:0000255"
FT   COILED          706..827
FT                   /evidence="ECO:0000255"
FT   COILED          879..916
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   971 AA;  113523 MW;  1C3B47BAD679CBDD CRC64;
     MLKLKGEFRT AKGLKDENKK QAQTLVFTDN QVEFKSNKQY HLRQLQQLKK KLLTLQQELE
     IRTQELQASY RSLLQYQSIL EKQTSDLLVL HHHCKLKEDE VILYEEEMGS HSKNTGEKLH
     LAQEQLALAG DKIVSLERSL NLYRDKYQTS LSNIELLECQ VKMLEEELSG LICQDPENKG
     DHSKVRIYTS PCMIQEHQET LKRLSEVWQK VSEQDDLIQE LRNKLACSNS LVLEREEALI
     KLRADFASYT ATHRHPPTSS EDCEDITKIL KYLQEQKDSQ CLHVEEYQNL VKDLRLELEA
     VSEQKKKIMK DMMKLELDLH GLREETSCVI EKKDKETVFL QYRLQDLQQQ YTESQKLSLK
     KDKLLQDKDE RLNELEKKLT QVQCLFLEKE TELEKLQSTT KELDANLQEV RQSTSKIDNE
     GLRSEIQKLK ESLEEAREQL RVSDQNLSQC KDEAHLSANN LEDAHRKLEN CLLQDKRKDD
     VIKDLQSQLQ KLQKESSETE EERKNNRQQL LELSSELNEG QRRLSSAEKE KSLLQKTLDE
     EEKKIDELLH GAKVSEQKQR ELTNSLSKLQ DELAETKRLL EEKREQLRKS KDQEKALEEE
     IEALRQESKK KEKMAKEQLR KLEEEKENLQ AELSSCSSQL DSSINKYNNS QKVIQELNTE
     IARQKDSIMI LQTQLDSAIQ KEKNCFQNMV SKETYEELLR KSGTCQDDLT QALEKLTQAT
     SETKSLQRNL QQTQERKAQL EDEIMAYEER MKKLNMELKK LQGFQQQSEL EVHNFDKKLE
     EMGNQVLQWQ RQHQSDLKML AAKETQLREF QEEMTALKEN LLADEKEPSL MPSKPAPKEN
     YRHHRENDQI MCNVEQWAKE QKLANEKLGN KLREQVKYIA KLTGEKDHLH NVMAHLQQEN
     KKLKNEIEEK KLKAGTPRIC AKVLGPCKLE PSQKGKLCGA LGWRGVCQDP LPKMDLTKYT
     GVPHCSGSSY C