AEGP_MOUSE
ID AEGP_MOUSE Reviewed; 1228 AA.
AC A2AJA7; A2AJA6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Apical endosomal glycoprotein;
DE AltName: Full=MAM domain-containing protein 4;
DE Flags: Precursor;
GN Name=Mamdc4 {ECO:0000312|MGI:MGI:2685841}; Synonyms=Aegp, Gm995;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Probably involved in the sorting and selective transport of
CC receptors and ligands across polarized epithelia.
CC {ECO:0000250|UniProtKB:Q63191}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2AJA7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AJA7-2; Sequence=VSP_026433;
CC -!- MISCELLANEOUS: [Isoform 1]: Gene prediction based on similarity to rat
CC ortholog.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM25169.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL732590; CAM25169.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL732590; CAM25170.1; -; Genomic_DNA.
DR AlphaFoldDB; A2AJA7; -.
DR SMR; A2AJA7; -.
DR STRING; 10090.ENSMUSP00000092735; -.
DR GlyGen; A2AJA7; 5 sites.
DR PhosphoSitePlus; A2AJA7; -.
DR PaxDb; A2AJA7; -.
DR PRIDE; A2AJA7; -.
DR Antibodypedia; 64043; 9 antibodies from 7 providers.
DR Ensembl; ENSMUST00000114223; ENSMUSP00000109861; ENSMUSG00000026941. [A2AJA7-1]
DR MGI; MGI:2685841; Mamdc4.
DR VEuPathDB; HostDB:ENSMUSG00000026941; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000162046; -.
DR InParanoid; A2AJA7; -.
DR PRO; PR:A2AJA7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AJA7; protein.
DR Bgee; ENSMUSG00000026941; Expressed in epithelium of small intestine and 118 other tissues.
DR ExpressionAtlas; A2AJA7; baseline and differential.
DR Genevisible; A2AJA7; MM.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 3.
DR CDD; cd06263; MAM; 6.
DR Gene3D; 4.10.400.10; -; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR000998; MAM_dom.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF00629; MAM; 6.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00192; LDLa; 3.
DR SMART; SM00137; MAM; 6.
DR SUPFAM; SSF49899; SSF49899; 6.
DR SUPFAM; SSF57424; SSF57424; 2.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 2.
DR PROSITE; PS50060; MAM_2; 6.
PE 3: Inferred from homology;
KW Alternative splicing; Disulfide bond; Glycoprotein; Membrane;
KW Protein transport; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1228
FT /note="Apical endosomal glycoprotein"
FT /id="PRO_0000286579"
FT TOPO_DOM 23..1159
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1160..1180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1181..1228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..49
FT /note="LDL-receptor class A 1; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 65..223
FT /note="MAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 229..267
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 270..426
FT /note="MAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 457..492
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 492..649
FT /note="MAM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 659..815
FT /note="MAM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 817..975
FT /note="MAM 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 977..1144
FT /note="MAM 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 641
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 841
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 230..242
FT /evidence="ECO:0000250|UniProtKB:P01130,
FT ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 237..255
FT /evidence="ECO:0000250|UniProtKB:P01130,
FT ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 249..266
FT /evidence="ECO:0000250|UniProtKB:P01130,
FT ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 458..469
FT /evidence="ECO:0000250|UniProtKB:P01130,
FT ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 465..482
FT /evidence="ECO:0000250|UniProtKB:P01130,
FT ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 476..491
FT /evidence="ECO:0000250|UniProtKB:P01130,
FT ECO:0000255|PROSITE-ProRule:PRU00124"
FT VAR_SEQ 578..656
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_026433"
SQ SEQUENCE 1228 AA; 134830 MW; AD4F60B903644BAB CRC64;
MCLPSHLLST WVLFMAAQSL GKTWLPNHCR SPIKAVCNFV CDCGDCSDET QCGFHGASTI
PSTSFTCNFE QDSCGWQDIS TSGYRWLRDR AGAVLHGPGP HSDHTHGTDL GWYMAVGTHS
GKEPSTATLR SPVMREAAPT CELRLWYHIA SRDVAELRLD LTHGVETLTL WQTSGPWGPG
WQELAVNTGR IQGDFKVTFS ATRNATHRGA VALDDVEFRD CGLPIPQARC PLGHHHCQNK
ACVEPHQLCD GEDNCGDRSD EDPLICSHHM ATDFETGLGP WNQLEGWTRN HSAGSMVSPA
WPHRDHSRNS AYGFFLISVA KPGTTAVLYS PEFQGSVSNN CSFTFYYYLH GSEASHFQLF
LQAQGLNTPQ VPVLLRSRHG ELGTAWVRDR VDIQSAHPFR ILLAGETGPG GVVGLDDLIM
SSHCMLVPAM STLQSSLSGP VPLALYPQTS IKLPQQTCEP GHLSCGDLCV PPEQLCDFQK
HCAEGEDEHK CGTTDFESAS AGGWEDISVG KLQWQWVEAQ EKSKPAGDAN RDAPGHFLSL
QKAWGQLRSE ARALTPALGP SGPHCELHMA YYFQSHPQGF LALVVVENGF RELLWQAPGG
GSGSWTEEKI ILGARRRPFQ LEFVSLVDLD GPGQQGAGVD NVTLRDCNPM VTTESDQELS
CNFERDSCSW HTGHLTDAHW HRIKSHGSQL DHTTGQGFFM FLDPTDPPAR GQGALLLTRP
QVPVVPKECL SFWYRLYGPQ IGTLCLAMRR EREEDILLWS RSGTHGNRWH QAWVTLHHQP
EASTKYQLLF EGLRNGYHGT MALDDIAVRP GPCWAPKSCS FEDSDCGFSP GGWGLWTHQS
NASGLASWGP WIDHTTGTAQ GHYMVVDTSP NVLPKGHVAA LTSEEHQPLS QPACLTFWYH
MSVPNPGTLR VHVEESTRRQ ELSISAHGRS AWRLGSVNVQ AEQAWKVVFE AVAAGVEYSY
MALDDISLQD GPCPQPGSCD FETGLCGWSH LPWPSLGGYS WDWSSGATPS RYPQPSVDHT
LGTEAGHFAF FETSVLGPGG QAAWLRSEPL PATTVSCLRF WYYMGFPEHF YKGELRVLLS
SARGQLAVWY QGGHLRDQWL QVQIELSNSE EFQIVFEATL GGQPALGPIA IDDVQYLAGQ
QCKQPSPSQG EVAAPVSVPV AVGGALLFFM FLVLMGLGGW HWLQKQHCPG QRSTDAAASG
FANILFNADH VTLPESITSN PQSPPDLA
