LMPA_DICDI
ID LMPA_DICDI Reviewed; 779 AA.
AC Q9XYS8; Q55FR1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Lysosome membrane protein 2-A;
DE AltName: Full=Lysosome membrane protein II-1;
DE Short=LIMP II-1;
GN Name=lmpA; ORFNames=DDB_G0267406;
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], AND SUBCELLULAR LOCATION.
RX PubMed=10189376; DOI=10.1083/jcb.145.1.167;
RA Karakesisoglou I., Janssen K.-P., Eichinger L., Noegel A.A., Schleicher M.;
RT "Identification of a suppressor of the Dictyostelium profilin-minus
RT phenotype as a CD36/LIMP-II homologue.";
RL J. Cell Biol. 145:167-181(1999).
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).
RN [3]
RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, GLYCOSYLATION, AND TOPOLOGY.
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).
CC -!- FUNCTION: May act as a lysosomal receptor (By similarity). May be
CC involved in macropinocytosis and fluid phase exocytosis. Binds to the
CC anionic phospholipid phosphoinositol 4,5-bisphosphate, but not to
CC phosphatidylcholine and only weakly to phosphatidylserine.
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:10189376, ECO:0000269|PubMed:11489884}.
CC -!- DEVELOPMENTAL STAGE: Found at all stages of development. Down-regulated
CC at the onset of aggregation, but small amounts are still detectable at
CC late stages of development (at protein level).
CC {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; AF124329; AAD25077.1; -; mRNA.
DR EMBL; AAFI02000003; EAL73155.1; -; Genomic_DNA.
DR RefSeq; XP_647472.1; XM_642380.1.
DR AlphaFoldDB; Q9XYS8; -.
DR STRING; 44689.DDB0191500; -.
DR PaxDb; Q9XYS8; -.
DR ABCD; Q9XYS8; 2 sequenced antibodies.
DR EnsemblProtists; EAL73155; EAL73155; DDB_G0267406.
DR GeneID; 8616279; -.
DR KEGG; ddi:DDB_G0267406; -.
DR dictyBase; DDB_G0267406; lmpA.
DR eggNOG; KOG3776; Eukaryota.
DR HOGENOM; CLU_358414_0_0_1; -.
DR InParanoid; Q9XYS8; -.
DR OMA; CALQQNN; -.
DR PhylomeDB; Q9XYS8; -.
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:Q9XYS8; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0032009; C:early phagosome; 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; IDA:dictyBase.
DR GO; GO:0044354; C:macropinosome; IDA:dictyBase.
DR GO; GO:0140220; C:pathogen-containing vacuole; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
DR GO; GO:0032010; C:phagolysosome; IDA:dictyBase.
DR GO; GO:0012506; C:vesicle membrane; IDA:dictyBase.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:dictyBase.
DR GO; GO:0005044; F:scavenger receptor activity; IBA:GO_Central.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IGI:dictyBase.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:dictyBase.
DR GO; GO:0001845; P:phagolysosome assembly; IDA:dictyBase.
DR GO; GO:0090383; P:phagosome acidification; IMP:dictyBase.
DR GO; GO:0044655; P:phagosome reneutralization; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IGI:dictyBase.
DR InterPro; IPR002159; CD36_fam.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR PANTHER; PTHR11923; PTHR11923; 1.
DR Pfam; PF01130; CD36; 2.
DR SUPFAM; SSF49842; SSF49842; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Lysosome; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..779
FT /note="Lysosome membrane protein 2-A"
FT /id="PRO_0000327757"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..732
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 733..753
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 754..779
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 771..774
FT /note="Tyrosine-type lysosomal sorting signal"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 619
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 651
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 693
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 779 AA; 87829 MW; 79FEB65E1F076233 CRC64;
MVKRGCCHRK MVNHKGCLVS GIFLAVIGAV LFILAFALLP HLINQTTQNA VIQAVIVDST
SSQRYNDWAG QQSIENYYQQ YFYAWNLTNP NEFLNGSIPI FETVGPFNYK YEFNFSNVTF
QDGGNLATYT QSKSFIYQSD MSPNDPNEIM ITNINPAYLG LMFQLAPNAE LLDNMPAENL
LIALSGCGQM RLFLEYLSSD NFTNIVYFTQ NPKLYQEQYL NILKSLNGDE QYFYQQWANA
TSIPQKGNGW YGMLVSSVNN NNESSNISIL SAKLLFNSSN ENSILNQEIG STLWINALLG
DKTSITVLTS ELQLTVDQID MILNWWLNDF SKVYTESYVN EICDIPDISM LGVCQFVTGN
ALNGRSISNY TFLTQPFDQG PIEIPLLYQS IGIDVKLSVS VQQAYKSLFN ESDSNSILNL
NGLVNFLTAS KSFDTFKQYN VTLFDAIKII GYATAELYEQ YNKPTILGLY EKYGGLIVTR
SMDDWLWNCQ DGILDYLGVD QPCALQQNNT VNKPSTIFTG QQDLSMTNQI FEFQEQTFLT
CWNGSVQVEG FTESGQFPPL QSDPPQTMTL FEENVIRPVQ LELSGDSQVQ GIDTKRYYLV
NNSFPISTTF KTTIPGFANL TDIQNLPIYV SLWDMYEVPP QYSSNNLQGL NQTYQSAQVP
LDLEPITGNA LYYNLKLQIN LAIPEFSNWF SSNSTFKNMK SNVFYPILKI GQTATPSQSN
IDLLNSQFKL IKILGFVPVI VVSIIGGIIL IAGISMFAFG FKKLRQQKQQ GYQAIINNE
