SAXO1_MACFA
ID SAXO1_MACFA Reviewed; 474 AA.
AC Q4R7D3;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Stabilizer of axonemal microtubules 1;
GN Name=SAXO1; Synonyms=FAM154A; ORFNames=QtsA-15565;
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].
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: 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}.
CC Cytoplasm, cytoskeleton, flagellum axoneme
CC {ECO:0000250|UniProtKB:Q8IYX7}. Note=In multi-ciliated cells, localizes
CC to the basal bodies and in non-ciliated cells, to the centrosome. In
CC spermatozoa, colocalizes with microtubules along the length of the
CC axoneme from its proximal end to its distal tip and with tubulin at the
CC distal end of the flagellum and at the proximal centriole.
CC {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE00989.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB168886; BAE00989.1; ALT_INIT; mRNA.
DR RefSeq; NP_001271034.1; NM_001284105.1.
DR AlphaFoldDB; Q4R7D3; -.
DR STRING; 9541.XP_005581717.1; -.
DR GeneID; 101925512; -.
DR CTD; 158297; -.
DR eggNOG; ENOG502QWHB; Eukaryota.
DR OrthoDB; 732196at2759; -.
DR Proteomes; UP000233100; 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: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; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Flagellum; Reference proteome; Repeat.
FT CHAIN 1..474
FT /note="Stabilizer of axonemal microtubules 1"
FT /id="PRO_0000089738"
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 318..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT REGION 444..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 54575 MW; 7661C677EBAFA992 CRC64;
MKTKCICELC SCGRHHCPHL PTKIYDKTEK PCLLSEYTEN YPCYHSYLPR ESFKPRREYQ
KGSIPMEGLT TSRRDFGPHK VAPVKAHQYD QFVPSEENMD LLTTYKKDYN PYTVCRVDPI
KPRDSKYPYS NKMEYLPTYK ADYLPWNQPR RQPLRLEHKY QPASVRFDNR TTHQDDYPIK
GLVKTVSCKP LAMPKLCNIP LEDVTNYKMS YVAHPVEKRF VHEAEKFRPC EIPFESLTTH
KQSYRGLMGE PAKSLKPLAR PPGLDMPFSN TTEFRDKYQA WPTPQMFSKA PITYVPPEDS
MDLLTTVQAH YTYPKGVPAR SCRPAPQIRK SGRFEGSSTT KDDYKQWSSM RTEPVKPIPQ
LDFPTEPLDC LTTTRAHYVP HPPINTKSCK PHWSGPRGNV PVEGQTTYTI SFTPKEMSKC
LASYPEPPGY TFEEVDALGH RIYKPVSQAG SQQSSHLSVD DSENPSQRKL EVSA
