ARL_SCHPO
ID ARL_SCHPO Reviewed; 186 AA.
AC Q09767;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=ADP-ribosylation factor-like protein alp41;
DE AltName: Full=Altered polarity protein 41;
GN Name=alp41; ORFNames=SPAC22F3.05c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=10683446; DOI=10.1016/s0014-5793(00)01202-3;
RA Radcliffe P.A., Vardy L., Toda T.;
RT "A conserved small GTP-binding protein Alp41 is essential for the cofactor-
RT dependent biogenesis of microtubules in fission yeast.";
RL FEBS Lett. 468:84-88(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Has a role in the cofactor-dependent pathway of microtubule
CC biogenesis. Required for growth polarity control.
CC {ECO:0000269|PubMed:10683446}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; AB031326; BAA83522.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA91070.1; -; Genomic_DNA.
DR PIR; T38186; S62420.
DR RefSeq; NP_593036.1; NM_001018435.2.
DR AlphaFoldDB; Q09767; -.
DR SMR; Q09767; -.
DR BioGRID; 278263; 3.
DR STRING; 4896.SPAC22F3.05c.1; -.
DR MaxQB; Q09767; -.
DR PaxDb; Q09767; -.
DR PRIDE; Q09767; -.
DR EnsemblFungi; SPAC22F3.05c.1; SPAC22F3.05c.1:pep; SPAC22F3.05c.
DR PomBase; SPAC22F3.05c; alp41.
DR VEuPathDB; FungiDB:SPAC22F3.05c; -.
DR eggNOG; KOG0073; Eukaryota.
DR HOGENOM; CLU_040729_12_3_1; -.
DR InParanoid; Q09767; -.
DR OMA; EHRGYKL; -.
DR PhylomeDB; Q09767; -.
DR BRENDA; 3.6.5.2; 5613.
DR PRO; PR:Q09767; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; ISM:PomBase.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0007021; P:tubulin complex assembly; ISO:PomBase.
DR CDD; cd04154; Arl2; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR045873; Arl2.
DR InterPro; IPR044612; ARL2/3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR PANTHER; PTHR45697; PTHR45697; 1.
DR Pfam; PF00025; Arf; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51417; ARF; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; GTP-binding; Lipoprotein; Microtubule; Myristate;
KW Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..186
FT /note="ADP-ribosylation factor-like protein alp41"
FT /id="PRO_0000207423"
FT BINDING 23..30
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 66..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 125..128
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 186 AA; 21236 MW; 18845CF6D0500C21 CRC64;
MGLLTILRQQ KLKEREVRVL LLGLDNAGKT TILKCLLNED VNEVSPTFGF QIRTLEVEGL
RFTIWDIGGQ KTLRNFWKNY FESTEAIIWV VDSLDDLRLE ECRNTLQELL VEEKLLFTSI
LVLANKSDVS GALSSEEISK ILNISKYKSS HWRIFSVSAL TGLNIKDAIS WLANDLKEIK
LGTIDY
