ID Q99648_HUMAN Unreviewed; 417 AA.
AC Q99648;
DT 01-MAY-1997, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1998, sequence version 2.
DT 27-MAR-2024, entry version 131.
DE RecName: Full=Septin-5 {ECO:0000256|ARBA:ARBA00018908};
DE Flags: Fragment;
GN Name=CDCrel-1 {ECO:0000313|EMBL:AAC39780.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAC39780.1};
RN [1] {ECO:0000313|EMBL:AAC39780.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8021244;
RA Yagi M., Edelhoff S., Disteche C.M., Roth G.J.;
RT "Structural characterization and chromosomal location of the gene encoding
RT human platelet glycoprotein Ib beta.";
RL J. Biol. Chem. 269:17424-17427(1994).
RN [2] {ECO:0000313|EMBL:AAC39780.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9022087; DOI=10.1172/JCI119188;
RA Zieger B., Hashimoto Y., Ware J.;
RT "Alternative expression of platelet glycoprotein Ib(beta) mRNA from an
RT adjacent 5' gene with an imperfect polyadenylation signal sequence.";
RL J. Clin. Invest. 99:520-525(1997).
RN [3] {ECO:0000313|EMBL:AAC39780.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9611266; DOI=10.1016/S0378-1119(98)00146-2;
RA Yagi M., Zieger B., Roth G.J., Ware J.;
RT "Structure and expression of the human septin gene HCDCREL-1.";
RL Gene 212:229-236(1998).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family.
CC {ECO:0000256|RuleBase:RU004560}.
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DR EMBL; AF006988; AAC39780.1; -; Genomic_DNA.
DR AlphaFoldDB; Q99648; -.
DR SMR; Q99648; -.
DR MaxQB; Q99648; -.
DR PeptideAtlas; Q99648; -.
DR ChiTaRS; SEPT5; human.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0017157; P:regulation of exocytosis; ISS:UniProtKB.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR PANTHER; PTHR18884; SEPTIN; 1.
DR PANTHER; PTHR18884:SF68; SEPTIN-5; 1.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRSR:PIRSR006698-
KW 2}; Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR006698-2}.
FT DOMAIN 89..362
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 211
FT /note="Important for dimerization"
FT /evidence="ECO:0000256|PIRSR:PIRSR006698-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAC39780.1"
SQ SEQUENCE 417 AA; 47622 MW; 7C80117C1F69D005 CRC64;
RPFPGDGGRG RLCRPPPRAP RAPATPRLWL GCGSGACPDC DAATAWGQFA QSGGWLGRPR
GSTIPRDIDK QYVGFATLPN QVHRKSVKKG FDFTLMVAGE SGLGKSTLVH SLFLTDLYKD
RKLLSAEERI SQTVEILKHT VDIEEKGVKL KLTIVDTPGF GDAVNNTECW KPITDYVDQQ
FEQYFRDESG LNRKNIQDNR VHCCLYFISP FGHGLRPVDV GFMKALHEKV NIVPLIAKAD
CLVPSEIRKL KERIREEIDK FGIHVYQFPE CDSDEDEDFK QQDRELKESA PFAVIGSNTV
VEAKGQRVRG RLYPWGIVEV ENQAHCDFVK LRNMLIRTHM HDLKDVTCDV HYENYRAHCI
QQMTSKLTQD SRMESPIPIL PLPTPDAETE KLIRMKDEEL RRMQEMLQRM KQQMQDQ
//
