ID   SAXO1_RAT               Reviewed;         462 AA.
AC   Q6AYP6;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Stabilizer of axonemal microtubules 1;
GN   Name=Saxo1; Synonyms=Fam154a;
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 [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in the regulation of cilium length.
CC       Stabilizes microtubules at low temperature.
CC       {ECO:0000250|UniProtKB:Q8IYX7}.
CC   -!- SUBUNIT: Associates with microtubules via the Mn regions.
CC       {ECO:0000250|UniProtKB:Q8IYX7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome, centriole {ECO:0000250|UniProtKB:Q8IYX7}.
CC       Cytoplasm, cytoskeleton, cilium basal body
CC       {ECO:0000250|UniProtKB:Q8IYX7}. Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000250|UniProtKB:Q8IYX7}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:Q8IYX7}. Note=In
CC       multi-ciliated cells, localizes to the basal bodies and in non-ciliated
CC       cells, to the centrosome. In spermatozoa, colocalizes with microtubules
CC       along the length of the axoneme from its proximal end to its distal tip
CC       and with tubulin at the distal end of the flagellum and at the proximal
CC       centriole. {ECO:0000250|UniProtKB:Q8IYX7}.
CC   -!- DOMAIN: The Mn regions are involved in microtubule-binding and
CC       stabilization at low temperature. They are required and sufficient for
CC       cilium targeting. {ECO:0000250|UniProtKB:Q8IYX7}.
CC   -!- DOMAIN: The N-terminal region (residues 1-29) might play a role in
CC       centriole retention. {ECO:0000250|UniProtKB:Q8IYX7}.
CC   -!- SIMILARITY: Belongs to the FAM154 family. {ECO:0000305}.
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DR   EMBL; BC078965; AAH78965.1; -; mRNA.
DR   RefSeq; NP_001014134.2; NM_001014112.2.
DR   AlphaFoldDB; Q6AYP6; -.
DR   STRING; 10116.ENSRNOP00000055963; -.
DR   PaxDb; Q6AYP6; -.
DR   GeneID; 317471; -.
DR   KEGG; rno:317471; -.
DR   UCSC; RGD:1549779; rat.
DR   CTD; 317471; -.
DR   RGD; 1549779; Saxo1.
DR   eggNOG; ENOG502QWHB; Eukaryota.
DR   InParanoid; Q6AYP6; -.
DR   OrthoDB; 732196at2759; -.
DR   PhylomeDB; Q6AYP6; -.
DR   TreeFam; TF319394; -.
DR   PRO; PR:Q6AYP6; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005879; C:axonemal microtubule; ISS:UniProtKB.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0031514; C:motile cilium; ISS:UniProtKB.
DR   GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR   GO; GO:0070417; P:cellular response to cold; ISS:UniProtKB.
DR   GO; GO:0009631; P:cold acclimation; ISS:UniProtKB.
DR   GO; GO:0045724; P:positive regulation of cilium assembly; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR   InterPro; IPR033336; SAXO1/2.
DR   PANTHER; PTHR31516; PTHR31516; 1.
PE   2: Evidence at transcript level;
KW   Cell projection; Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW   Reference proteome; Repeat.
FT   CHAIN           1..462
FT                   /note="Stabilizer of axonemal microtubules 1"
FT                   /id="PRO_0000089739"
FT   REGION          30..64
FT                   /note="Mn 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYX7"
FT   REGION          65..97
FT                   /note="Mn 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYX7"
FT   REGION          98..131
FT                   /note="Mn 3"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYX7"
FT   REGION          132..165
FT                   /note="Mn 4"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYX7"
FT   REGION          166..199
FT                   /note="Mn 5"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYX7"
FT   REGION          200..232
FT                   /note="Mn 6"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYX7"
FT   REGION          233..266
FT                   /note="Mn 7"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYX7"
FT   REGION          267..299
FT                   /note="Mn 8"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYX7"
FT   REGION          300..332
FT                   /note="Mn 9"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYX7"
FT   REGION          333..366
FT                   /note="Mn 10"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYX7"
FT   REGION          367..400
FT                   /note="Mn 12"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYX7"
FT   REGION          401..434
FT                   /note="Mn 12"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYX7"
SQ   SEQUENCE   462 AA;  53265 MW;  FF2457E6B7604B72 CRC64;
     MNRKCICDLC SCGKHHCPHL PTKIYEKTEK PCFFSEYTEK YPTYLSYVPR ESFKPKLEYQ
     KVNIPMEGLS TTKRDFGTFN IVPVKHHLPE KATPIQDEMD FLTTYNQHYN YCPANRVNPI
     KPRDNKHQCN DKMECVPTYK ADYLPWNQQK RSSIRPPQSY RPASCRFDHR TTHQDDYPIK
     NPVDTVSYKP PHGPKLCNIP LESMTSYKSS YVAHPMEKRC VYEGEKYKPS EVPFDSLTTH
     KDSYRGLIGE PAKTWKPAPN HPGLDIPFPS NTEFREKFQP WPTPKIVPKE SIAYIPPEGK
     MDLLTTVQAD YKCPNGVPAQ SCRPVIHLKK SDRFESSTTN REDFKHWANI RREPVKPNHQ
     LKFSDEPMEY MTTNRAHYVP HAPANTKSCK PTWSGPRVNI PLEGQTTYST SFTPKEIQRC
     PASYPEPPGY IFDEVDAVGH RLYRPASGAT SQESNHLGFG DA