LMPC_DICDI
ID LMPC_DICDI Reviewed; 782 AA.
AC Q55FQ9; Q9BKJ8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Lysosome membrane protein 2-C;
DE AltName: Full=Lysosome membrane protein II-3;
DE Short=LIMP II-3;
GN Name=lmpC; ORFNames=DDB_G0267440;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION,
RP GLYCOSYLATION, AND TOPOLOGY.
RC STRAIN=AX4;
RX PubMed=11489884; DOI=10.1074/jbc.m103384200;
RA Janssen K.-P., Rost R., Eichinger L., Schleicher M.;
RT "Characterization of CD36/LIMPII homologues in Dictyostelium discoideum.";
RL J. Biol. Chem. 276:38899-38910(2001).
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: May act as a lysosomal receptor (By similarity). May be
CC involved role in macropinocytosis and fluid phase exocytosis.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}. Note=Localizes to membranes of
CC endolysosomal vesicles and macropinosomes.
CC {ECO:0000269|PubMed:11489884}.
CC -!- DEVELOPMENTAL STAGE: Found at all stages of development in comparable
CC quantities (at protein level). {ECO:0000269|PubMed:11489884}.
CC -!- PTM: Heavily glycosylated. {ECO:0000269|PubMed:11489884}.
CC -!- SIMILARITY: Belongs to the CD36 family. {ECO:0000305}.
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DR EMBL; AF238325; AAK30041.1; -; mRNA.
DR EMBL; AAFI02000003; EAL73172.1; -; Genomic_DNA.
DR RefSeq; XP_647474.1; XM_642382.1.
DR AlphaFoldDB; Q55FQ9; -.
DR STRING; 44689.DDB0191198; -.
DR PaxDb; Q55FQ9; -.
DR ABCD; Q55FQ9; 4 sequenced antibodies.
DR EnsemblProtists; EAL73172; EAL73172; DDB_G0267440.
DR GeneID; 8616281; -.
DR KEGG; ddi:DDB_G0267440; -.
DR dictyBase; DDB_G0267440; lmpC.
DR eggNOG; KOG3776; Eukaryota.
DR HOGENOM; CLU_358414_0_0_1; -.
DR InParanoid; Q55FQ9; -.
DR OMA; NNTIFKP; -.
DR PhylomeDB; Q55FQ9; -.
DR Reactome; R-DDI-114608; Platelet degranulation.
DR Reactome; R-DDI-434313; Intracellular metabolism of fatty acids regulates insulin secretion.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:Q55FQ9; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; HDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
DR GO; GO:0032010; C:phagolysosome; HDA:dictyBase.
DR GO; GO:0012506; C:vesicle membrane; IBA:GO_Central.
DR GO; GO:0005044; F:scavenger receptor activity; IBA:GO_Central.
DR GO; GO:0006911; P:phagocytosis, engulfment; IBA:GO_Central.
DR InterPro; IPR002159; CD36_fam.
DR PANTHER; PTHR11923; PTHR11923; 1.
DR Pfam; PF01130; CD36; 2.
DR PRINTS; PR01609; CD36FAMILY.
PE 1: Evidence at protein level;
KW Glycoprotein; Lysosome; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..782
FT /note="Lysosome membrane protein 2-C"
FT /id="PRO_0000327759"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..739
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 740..760
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 761..782
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 777..781
FT /note="Tyrosine-type lysosomal sorting signal"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 595
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 613
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 646
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 692
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 5
FT /note="N -> T (in Ref. 1; AAK30041)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 782 AA; 87876 MW; 5FA958647B487976 CRC64;
MVANNKGLLI AGLLLSVIGA ALFVISLALL PSVLNVATNN AIVDAVIVDS FKSQRYNDWA
GQKSVDNYFK QYYYLWNLTN PNEVLNGKNC NFEKIGPFNY KYEWNNSKVS FSDDGNLINY
IQSKSYKWIE GEDSLNPFTV STTNFNPAYL GLLSTLSKNS ITLGMTAEDL LYTLASAPQT
KQFLEYLSSD NFTMIAYFYN GPKYFNQQYQ LLLSTINNNL TTTPTIYFLE QWSNSTIIPT
NGNSSLWDNM LISYGLDSPS GISLQSALEI LNPMNQYSLL NSTNGISYWI NAVFNGPNSN
SYQILEQELG INQAQLTLVM IWWLKGFNDQ YTMSQLLKQC EIESIELLGV CQFITTIPLG
YKSISQFNIT NLPWLEPIEI PIAMGTNLTI STNEAQSNLF NDSIDDSLLT IHGLGLFLEQ
MSTNSNNFTK WNLTNNDAMT MIGYFLSYIP NTTGYSIKSV QSFYNTSGLI VTRTANEWLW
DCQDDLLDYL GIDQQCSFQQ NNTIFKPSTV YTGKKDLSLT NQYQQFQEQS TLTIWNGTVN
VTGFVENGQM APLVQDNLPQ SLTIFEENIL RPLSLVHSSS SSVMGVSTQR YYLPNQSFPI
DPVFNNSING FANLTGLFNG VPIYVSLWDM YGVPIEYSSL YINGLNQTYE NAEIPLDLEP
ITGNTLYYNL KLQINLQIPS NANSLWFSSL GNWTNIFSPT NSNSFGIFYP SLKIGQTATA
STNDINLLKQ QFKQIQTVKI APVVVVSIFG GILLIAGLVM AINGFRKTFY NNNQYNGYNI
IN
