AEGP_RAT
ID AEGP_RAT Reviewed; 1216 AA.
AC Q63191;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Apical endosomal glycoprotein;
DE AltName: Full=MAM domain-containing protein 4;
DE Flags: Precursor;
GN Name=Mamdc4; Synonyms=Aegp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-27; 108-121; 159-179;
RP 210-227 AND 270-279, AND TISSUE SPECIFICITY.
RC TISSUE=Intestinal epithelium;
RX PubMed=7829488; DOI=10.1074/jbc.270.4.1583;
RA Speelman B.A., Allen K., Grounds T.L., Neutra M.R., Kirchhausen T.,
RA Wilson J.M.;
RT "Molecular characterization of an apical early endosomal glycoprotein from
RT developing rat intestinal epithelial cells.";
RL J. Biol. Chem. 270:1583-1588(1995).
CC -!- FUNCTION: Probably involved in the sorting and selective transport of
CC receptors and ligands across polarized epithelia.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Apical endosomal tubules of developing rat
CC intestinal epithelial cells. {ECO:0000269|PubMed:7829488}.
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DR EMBL; L37380; AAA65200.1; -; mRNA.
DR PIR; A55620; A55620.
DR RefSeq; NP_665711.1; NM_145768.1.
DR AlphaFoldDB; Q63191; -.
DR SMR; Q63191; -.
DR STRING; 10116.ENSRNOP00000022390; -.
DR GlyGen; Q63191; 6 sites.
DR PaxDb; Q63191; -.
DR PRIDE; Q63191; -.
DR GeneID; 252882; -.
DR KEGG; rno:252882; -.
DR UCSC; RGD:708583; rat.
DR CTD; 158056; -.
DR RGD; 708583; Mamdc4.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q63191; -.
DR OrthoDB; 72691at2759; -.
DR PhylomeDB; Q63191; -.
DR PRO; PR:Q63191; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005768; C:endosome; IDA:RGD.
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; 2.
DR CDD; cd06263; MAM; 5.
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; 2.
DR SMART; SM00137; MAM; 5.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Membrane;
KW Protein transport; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:7829488"
FT CHAIN 22..1216
FT /note="Apical endosomal glycoprotein"
FT /id="PRO_0000020634"
FT TOPO_DOM 22..1155
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1156..1176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1177..1216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..54
FT /note="LDL-receptor class A 1; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 62..224
FT /note="MAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 229..269
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 268..427
FT /note="MAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 454..491
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 492..647
FT /note="MAM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 654..813
FT /note="MAM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 812..973
FT /note="MAM 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 972..1142
FT /note="MAM 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
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 639
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 839
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 231..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 238..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 250..267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 456..467
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 463..480
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 474..489
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1216 AA; 133777 MW; 64F3B28A7B61BA2E CRC64;
MCLPSCLLSI WVLFMAAQSL GKTWVPDHCR SPTEATCNFV CDCGDCSDEA QCGFHGASTT
PNTPFTCNFE QDPCGWQDIS TSGYRWLRDR AGAGLDSSGP HSDHTRGTDL GWYMAVGTHS
GKEPSTRTLR SPVMREAAPT CELRLWYHTD SRDVAELRLD LTHGMETLTL WQSSGPWGPW
PGRELAVNTG RIQGDFKVTF SATRNATHRG AVALDDMEFW DCGLPIPQAR CPLGHHHCQN
KACVEPHQLC DGEDNCGDSS DEDPLICSHH MATDFETGLG PWTQLEGWTR NFSAGSMVSP
AWPHRDHSRN SAYGFFLVSV AKPGTTAVLY SPEFQGSVSY NCSFTFYYYL HGSEANQFQL
FVQAQGLNTT QPPVLLRSRH GELGTAWVRD RVNIQSAHPF RILLAGETGP GGFVGLDDLI
MSNHCILVPG MSTLQSSLSG PVPLALYPQT SIKRTCDAGH LSCDELCVPP EQLCDFQQHC
AEGEDEEKCG TTDFESASAG GWEDISIGKL QWQRAEAQES GKPARDTNRN APGHFLSLRK
AWGQLRSEAR ALTPTLGPSG PHCELHMTYY FHSHPQGFLA LAVVENGFRE LLWQAPSSSS
GGWTLQKILL GARRWPFQLE FVSLVDLDGP GQQGAGVDNV TLRDCNPMVT TESDQEVSCN
FERDSCSWHT GHLTDAHWHR VKSHGSQYDH TTGQGFFMFL DPMDPPARGQ GALLLTRPQV
PVVPKECLSF WYHLHGPQIG TLCLAMRREG EEDTLLWSRS GTHGNRWHQA WVTLHHQLQP
STKYQLLFEG LRDGYHGTMG LDDMAVRPGP CWAAKRCSFE DSDCGFSPGD WGLWTRQNNA
SGLGPWGPWI DHTTGTAQGH YMVVDTSPNL LPKGHVASLT SEEHPPLSRP ACLSFWYHLS
FHNPGTLRVF VEESTRRQEL SISGHGGFAW RLGSVNVQAE QAWKVVFEAM ASGVEHSYMA
LDDISLQDGP CAQPGSCDFE SGLCGWSHLP WPGLGGYSWD WSSGATPSRY PRPSVDHTVG
TEAGHFAFFE TSVLGPGGQA AWLGSEPLPA TAVSCLHFWY YMGFPAHFYK GELRVLLSST
QGQLAVWHRG GHLRDQWLQV QIEVSSSEEF QIVFEATLGG QPALGPIALD DVEYLAGQHC
KQPTPSQGRV AAPVSVPVAV GGALLLFLLL LGLGGWHWLQ KQHLPCQSTD AAASGFDNIL
FNADQVTLPE SITSNP
