SEC2_CANAL
ID SEC2_CANAL Reviewed; 751 AA.
AC Q5AL49; A0A1D8PFJ3; Q5ALH3;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Rab guanine nucleotide exchange factor SEC2;
DE AltName: Full=GDP-GTP exchange factor SEC2;
GN Name=SEC2; OrderedLocusNames=CAALFM_C112970CA;
GN ORFNames=CaO19.12394, CaO19.4928;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP PHOSPHORYLATION AT SER-584 AND SER-598, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=20639857; DOI=10.1038/emboj.2010.158;
RA Bishop A., Lane R., Beniston R., Chapa-y-Lazo B., Smythe C., Sudbery P.;
RT "Hyphal growth in Candida albicans requires the phosphorylation of Sec2 by
RT the Cdc28-Ccn1/Hgc1 kinase.";
RL EMBO J. 29:2930-2942(2010).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=20693302; DOI=10.1128/ec.00109-10;
RA Jones L.A., Sudbery P.E.;
RT "Spitzenkorper, exocyst, and polarisome components in Candida albicans
RT hyphae show different patterns of localization and have distinct dynamic
RT properties.";
RL Eukaryot. Cell 9:1455-1465(2010).
CC -!- FUNCTION: Guanine nucleotide exchange factor for SEC4, catalyzing the
CC dissociation of GDP from SEC4 and also potently promoting binding of
CC GTP. Activation of SEC4 by SEC2 is needed for the directed transport of
CC vesicles to sites of exocytosis (By similarity). Required for
CC filamentous growth. {ECO:0000250, ECO:0000269|PubMed:20639857}.
CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000250}. Bud tip {ECO:0000250}.
CC Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:20639857,
CC ECO:0000269|PubMed:20693302}. Note=Localizes to the spitzenkorper, a
CC structure found in fungal hyphae which is the organizing center for
CC hyphal growth and morphogenesis.
CC -!- PTM: Phosphorylated at Ser-584 and Ser-598. Phosphorylation at Ser-584
CC by the CDC28-CCN1 and CDC28-HGC1 complexes is required to support
CC hyphal growth. In stationary phase and growing yeast cells, is
CC constitutively phosphorylated, probably on more than one residue, but
CC the pattern of phosphorylation rapidly changes upon hyphal induction
CC and precedes the appearance of hyphal germ tubes.
CC {ECO:0000269|PubMed:20639857}.
CC -!- SIMILARITY: Belongs to the SEC2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP017623; AOW26911.1; -; Genomic_DNA.
DR RefSeq; XP_722139.2; XM_717046.2.
DR AlphaFoldDB; Q5AL49; -.
DR SMR; Q5AL49; -.
DR BioGRID; 1219196; 1.
DR IntAct; Q5AL49; 1.
DR MINT; Q5AL49; -.
DR STRING; 237561.Q5AL49; -.
DR iPTMnet; Q5AL49; -.
DR PRIDE; Q5AL49; -.
DR GeneID; 3636119; -.
DR KEGG; cal:CAALFM_C112970CA; -.
DR CGD; CAL0000197956; SEC2.
DR VEuPathDB; FungiDB:C1_12970C_A; -.
DR eggNOG; KOG4324; Eukaryota.
DR HOGENOM; CLU_423355_0_0_1; -.
DR InParanoid; Q5AL49; -.
DR OrthoDB; 619794at2759; -.
DR PRO; PR:Q5AL49; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0051286; C:cell tip; IBA:GO_Central.
DR GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR GO; GO:0005934; C:cellular bud tip; IEA:UniProtKB-SubCell.
DR GO; GO:0070319; C:Golgi to plasma membrane transport vesicle; IDA:CGD.
DR GO; GO:0031521; C:spitzenkorper; IDA:CGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0030448; P:hyphal growth; IMP:CGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR040351; RAB3IL/RAB3IP/Sec2.
DR InterPro; IPR009449; Sec2_N.
DR PANTHER; PTHR14430; PTHR14430; 1.
DR Pfam; PF06428; Sec2p; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasmic vesicle; Guanine-nucleotide releasing factor;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..751
FT /note="Rab guanine nucleotide exchange factor SEC2"
FT /id="PRO_0000424363"
FT REGION 326..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 22..162
FT /evidence="ECO:0000255"
FT COMPBIAS 565..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 584
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:20639857"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20639857"
SQ SEQUENCE 751 AA; 85334 MW; 057F047900E253E6 CRC64;
MSSQADYDKR LAEEVGSLST RLVTAVNKQV ELEETILELR KQVSALKLKN EQLNQSDIKL
KTILPKYIKL QDDYRETLTK KKEAESQNTK LQGEVEDLTA SLFDEANTMV SNASRETHNF
KIKNRKLYEE LDEKNIIIND LQEQLQDLKQ MFIKMEEQSK IQSYSQSNTP KIESSTDFNE
TNSIHTNTNF SESKLSKYNT RSTLGDEESQ NYNLQQLQRI IYSPLITSIR FDLNNYNIDF
KGFVYQLIKP DFQFDLSHLK TIPFFKSIWQ SEIENCIHYI PSLPATTTLL NRWQKGKTFW
GSLIEGKVSI EPIKGSNETF KLTYKGNNAS GNSSNENTES ISNRSSATGS VVPVAIKDPC
TFCGEARNDS LEHCRLYHLK LFESNTANNS GNNSTNQDQQ GNNDNTHVIA SYPLCNYCLI
KLRNLCDFFA KIRLIRSNIF KLKQNDSFDE FIVVPGSFGQ FKRSNTISNR NGTYSSSSTS
SSSTSSVSSS SATTANGESL NSTTHNIQLE RTEESKLIKL YIMMLLIRSK IFWSKLGFWD
TIDQINEINL DEIHYEAFSY LIPKPTQQQQ QQQGDIRSQS NFNSPRQSVD GRSVLSGSIS
SPRQPNLDKQ QKDSIVDETV AQLQRDGVVR SETASAEEKF EDAISDETNG QEQLRSEKLQ
TGKTVTEPNS VSESEPVQEP EQVRSKSNNN TNNKNKDTKI EDSDAEHTFS LKRSHSKQFK
DQLNKELDQT LEMLAENIDF DESSNGNGNG N
