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PSIF_DICDI
ID   PSIF_DICDI              Reviewed;         708 AA.
AC   Q7YSJ4; Q54YZ8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Protein psiF;
DE   AltName: Full=Discoidin-inducing complex subunit A;
DE   Flags: Precursor;
GN   Name=psiF; Synonyms=dicA, dicA1; ORFNames=DDB_G0278581;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF N-TERMINUS,
RP   PROTEIN SEQUENCE OF 625-638, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=15947191; DOI=10.1128/ec.4.6.991-998.2005;
RA   Kolbinger A., Gao T., Brock D., Ammann R., Kisters A., Kellermann J.,
RA   Hatton D., Gomer R.H., Wetterauer B.;
RT   "A cysteine-rich extracellular protein containing a PA14 domain mediates
RT   quorum sensing in Dictyostelium discoideum.";
RL   Eukaryot. Cell 4:991-998(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Acts as a quorum sensing protein regulating discoidin gene
CC       expression during growth and development. D.discoideum is a single-
CC       celled amoebae and switches to multicellular development when food
CC       becomes limited. As the growing cells reach a high density, they begin
CC       expressing discoidin genes. The ability of psiF/dicA to induce
CC       discoidin gene expression when present in conditioned medium, suggests
CC       that it allow cells to sense their local density.
CC       {ECO:0000269|PubMed:15947191}.
CC   -!- SUBUNIT: Forms a complex with dicB. {ECO:0000269|PubMed:15947191}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:15947191}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in vegetative and developing cells.
CC       {ECO:0000269|PubMed:15947191}.
CC   -!- MISCELLANEOUS: According to PubMed:15947191, it is secreted in the
CC       conditioned medium. However, prediction tools clearly predict a
CC       transmembrane domain. In some conditions, it may be cleaved and
CC       secreted in the conditioned medium, which would explain the
CC       discrepancy.
CC   -!- SIMILARITY: Belongs to the prespore-cell-inducing factor family.
CC       {ECO:0000305}.
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DR   EMBL; AJ548837; CAD69024.1; -; mRNA.
DR   EMBL; AJ548838; CAD69025.1; -; Genomic_DNA.
DR   EMBL; AAFI02000023; EAL68463.1; -; Genomic_DNA.
DR   RefSeq; XP_642054.1; XM_636962.1.
DR   AlphaFoldDB; Q7YSJ4; -.
DR   PaxDb; Q7YSJ4; -.
DR   EnsemblProtists; EAL68463; EAL68463; DDB_G0278581.
DR   GeneID; 8621266; -.
DR   KEGG; ddi:DDB_G0278581; -.
DR   dictyBase; DDB_G0278581; psiF.
DR   eggNOG; ENOG502RA06; Eukaryota.
DR   HOGENOM; CLU_024170_0_0_1; -.
DR   InParanoid; Q7YSJ4; -.
DR   OMA; TCSYYDY; -.
DR   PhylomeDB; Q7YSJ4; -.
DR   PRO; PR:Q7YSJ4; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005576; C:extracellular region; IDA:dictyBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   InterPro; IPR011874; Fibro_Slime.
DR   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   InterPro; IPR001673; S_mold_repeat.
DR   Pfam; PF00526; Dicty_CTDC; 3.
DR   Pfam; PF07691; PA14; 1.
DR   SMART; SM00758; PA14; 1.
DR   TIGRFAMs; TIGR02148; Fibro_Slime; 1.
DR   PROSITE; PS51820; PA14; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Differentiation; Direct protein sequencing;
KW   Glycoprotein; Membrane; Reference proteome; Secreted; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:15947191"
FT   CHAIN           20..708
FT                   /note="Protein psiF"
FT                   /id="PRO_0000327558"
FT   TOPO_DOM        20..643
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        644..664
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        665..708
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          103..263
FT                   /note="PA14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT   REGION          682..708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        317
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        371
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        498
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        600
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   708 AA;  76482 MW;  CEEC0F6A5F7B1190 CRC64;
     MKYLFIAIIL ILYCSFTKAD QKKFLVNMYD NDPLFSPDFE NANGAQTGLV KKKLGSDGKP
     IPANYDMKDP NGNYYIKNAT TFKSWFNEVA GVSILVPFEL VLTQTAGSQN YYSYSNTSFF
     PLNELGWYNP SIKGDYEFKK YQDSNKKEQN FHFCMHASFI MSTNCKEVFK FKGDDDVWVF
     INDVLVLDIG GVHGVQDGTV DMANLPEKIH DSTNSKLGNC KNGTYPFDFF YCERHTKASN
     CLFETNMGFT CSYYDYCGIC NGKGECCTDV KLNQCYTKKC PLPNSLPNGA TNYQDYMTIV
     PTNTCGGTDK CKIYSCNNST GCEFKQKSCD DGDKCTKDAC DSKTGYCSNI PTNPSVVTSC
     LKSGCDSTTG NYSTPTNCDD KDPCTIDSCI NGQGCVHTKA CDDEDPCTTD SCSADGKCTH
     TAIAKCNSDC PSCPSKKCKI TSCSEDSGAC NYVDMVFASP SECYKATCDP ETEEAIYSPI
     DSSCDTSDSC FTAQCNLNKT CTRVPAINCD DNNECTTDSC SGGSCSNTAI ACDDNDPCTI
     DTCSPSEGCI FTPIVCEQTS LCNTFTCSVG KCVPTPITCS SSVKCQDSIC REGVGCVYFN
     RTCPPDDDCS SAYCSMETGK CISKAYDPLP FSCQSTAVKV GVGIGAAAAA GIAIGGAVAA
     GLAIFGGKKA YDTWKTSRGN VMTGSQSNPL YTQNQNNGNN PLYSAPAE
 
 
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