NICA_DICPU
ID NICA_DICPU Reviewed; 643 AA.
AC F0ZBA6;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Nicastrin {ECO:0000303|PubMed:25197054};
DE Short=DpNCT {ECO:0000303|PubMed:25197054};
DE Flags: Precursor;
GN Name=ncstn {ECO:0000250|UniProtKB:Q54JT7};
GN ORFNames=DICPUDRAFT_96800 {ECO:0000312|EMBL:EGC38810.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000312|Proteomes:UP000001064};
RN [1] {ECO:0000312|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000312|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
RN [2] {ECO:0007744|PDB:4R12}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 19-611, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-96; ASN-166; ASN-333; ASN-385 AND ASN-584.
RX PubMed=25197054; DOI=10.1073/pnas.1414837111;
RA Xie T., Yan C., Zhou R., Zhao Y., Sun L., Yang G., Lu P., Ma D., Shi Y.;
RT "Crystal structure of the gamma-secretase component nicastrin.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:13349-13354(2014).
CC -!- FUNCTION: Essential subunit of the gamma-secretase complex, an
CC endoprotease complex that catalyzes the intramembrane cleavage of
CC integral membrane proteins such as Notch receptors and APP (amyloid-
CC beta precursor protein). {ECO:0000250|UniProtKB:Q92542}.
CC -!- SUBUNIT: Component of the gamma-secretase complex, a complex composed
CC of a presenilin homodimer, nicastrin, aph1 and pen2.
CC {ECO:0000250|UniProtKB:Q92542}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the nicastrin family. {ECO:0000305}.
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DR EMBL; GL870969; EGC38810.1; -; Genomic_DNA.
DR RefSeq; XP_003284704.1; XM_003284656.1.
DR PDB; 4R12; X-ray; 1.95 A; A=19-611.
DR PDBsum; 4R12; -.
DR AlphaFoldDB; F0ZBA6; -.
DR SMR; F0ZBA6; -.
DR STRING; 5786.XP_003284704.1; -.
DR EnsemblProtists; EGC38810; EGC38810; DICPUDRAFT_96800.
DR GeneID; 10506558; -.
DR KEGG; dpp:DICPUDRAFT_96800; -.
DR eggNOG; KOG2657; Eukaryota.
DR InParanoid; F0ZBA6; -.
DR OMA; CMRRNSI; -.
DR OrthoDB; 777987at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:EnsemblProtists.
DR GO; GO:0070765; C:gamma-secretase complex; IEA:EnsemblProtists.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:EnsemblProtists.
DR GO; GO:0044351; P:macropinocytosis; IEA:EnsemblProtists.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006909; P:phagocytosis; IEA:EnsemblProtists.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0044671; P:sorocarp spore cell differentiation; IEA:EnsemblProtists.
DR DisProt; DP02165; -.
DR InterPro; IPR041084; Ncstrn_small.
DR InterPro; IPR008710; Nicastrin.
DR PANTHER; PTHR21092; PTHR21092; 1.
DR Pfam; PF18266; Ncstrn_small; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Membrane;
KW Notch signaling pathway; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..643
FT /note="Nicastrin"
FT /evidence="ECO:0000255"
FT /id="PRO_5003262286"
FT TOPO_DOM 21..611
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 612..632
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 633..643
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25197054,
FT ECO:0007744|PDB:4R12"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25197054,
FT ECO:0007744|PDB:4R12"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25197054,
FT ECO:0007744|PDB:4R12"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25197054,
FT ECO:0007744|PDB:4R12"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25197054,
FT ECO:0007744|PDB:4R12"
FT DISULFID 42..54
FT /evidence="ECO:0000269|PubMed:25197054,
FT ECO:0007744|PDB:4R12"
FT DISULFID 204..210
FT /evidence="ECO:0000269|PubMed:25197054,
FT ECO:0007744|PDB:4R12"
FT DISULFID 308..318
FT /evidence="ECO:0000269|PubMed:25197054,
FT ECO:0007744|PDB:4R12"
FT DISULFID 479..486
FT /evidence="ECO:0000269|PubMed:25197054,
FT ECO:0007744|PDB:4R12"
FT DISULFID 540..551
FT /evidence="ECO:0000269|PubMed:25197054,
FT ECO:0007744|PDB:4R12"
FT DISULFID 546..556
FT /evidence="ECO:0000269|PubMed:25197054,
FT ECO:0007744|PDB:4R12"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:4R12"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 215..225
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:4R12"
FT TURN 252..255
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 256..270
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 279..288
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 294..305
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 327..331
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 337..343
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:4R12"
FT TURN 353..356
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 357..368
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 370..380
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 388..392
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 403..407
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 415..420
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:4R12"
FT TURN 428..431
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 442..444
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 445..459
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 470..481
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 518..530
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 533..537
FT /evidence="ECO:0007829|PDB:4R12"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 549..552
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 555..558
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 560..566
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 571..574
FT /evidence="ECO:0007829|PDB:4R12"
FT TURN 575..578
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 579..583
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 590..593
FT /evidence="ECO:0007829|PDB:4R12"
FT STRAND 599..604
FT /evidence="ECO:0007829|PDB:4R12"
SQ SEQUENCE 643 AA; 72508 MW; 37662BD524B3D43A CRC64;
MRFKNVLVLL LLLVFSVINS EPSAPATISD NIYTTLYSSY PCTKIMTSDG QFGCSSKHGG
NSGILYLIDD DESYNNYFSY SQQKDIIVVL DTNYFNSTSV LNLHNKSKIE GIIVLTDTKK
TYPYSPDSRY PNKIYGLYPN SNLEWNPNAD GFTYFSFPFP IFAIDNQTSV AIRNVSKHNR
DGQYPAWGAE LDSFMQGAIN SETCLRRGFC EPVGGQSIWS SFSSKIDKEK EIILVMLPFD
TTAFFRDLSI GADQSSFATV TLLSVIKSLA AVDRSSWNKE VVFAFWNAER WGYVGSEYFI
NDLLNFQCKT YNSDKSKCID PPRADLAFQT QINFTKISTI IELNQIGRAQ LDKNLGKYSL
YLHTAGTKTS SVTDILDQVA SSYENSTITF KPTTQTELPP SSSMSFLKKT NKIPVVVITD
HDYKYSNPYY GYEQDDNENV LGSTLNDIVY ILSTFIDRIA GGNNNITIDK NFINILYPCF
TSSITCFNIL MKTYPLNEVP NFYSSVFGTS LTTTLSPYET KLIHRLLYSI TQYNSTLTNC
TSDNDCPSSL CYSGQCVSSN THLHNALSLG FDFDTSKNVW KIVNSSYPIF TESNWDYTAL
KVFKIGNSTT EIWFLVSGLI ELLVSIGLIL YVKKFLSNRY KLL
