AMNLS_PIG
ID AMNLS_PIG Reviewed; 519 AA.
AC F1SAM7;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 2.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Protein amnionless;
DE Contains:
DE RecName: Full=Soluble protein amnionless;
DE Flags: Precursor;
GN Name=AMN;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000312|Proteomes:UP000008227};
RN [1] {ECO:0000312|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc;
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH CUBN, FUNCTION,
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=30523278; DOI=10.1038/s41467-018-07468-4;
RA Larsen C., Etzerodt A., Madsen M., Skjodt K., Moestrup S.K.,
RA Andersen C.B.F.;
RT "Structural assembly of the megadalton-sized receptor for intestinal
RT vitamin B12 uptake and kidney protein reabsorption.";
RL Nat. Commun. 9:5204-5204(2018).
CC -!- FUNCTION: Membrane-bound component of the endocytic receptor formed by
CC AMN and CUBN (PubMed:30523278). Required for normal CUBN glycosylation
CC and trafficking to the cell surface. The complex formed by AMN and CUBN
CC is required for efficient absorption of vitamin B12. Required for
CC normal CUBN-mediated protein transport in the kidney (By similarity).
CC {ECO:0000250|UniProtKB:Q9BXJ7, ECO:0000269|PubMed:30523278}.
CC -!- SUBUNIT: Interacts (via extracellular region) with CUBN/cubilin, giving
CC rise to a huge complex containing one AMN chain and three CUBN chains.
CC {ECO:0000269|PubMed:30523278}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:Q9BXJ7}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q9BXJ7}. Cell membrane
CC {ECO:0000305|PubMed:30523278}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q9BXJ7}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q9BXJ7}. Membrane, coated pit
CC {ECO:0000250|UniProtKB:Q9BXJ7}.
CC -!- TISSUE SPECIFICITY: Detected in kidney cortex (at protein level).
CC {ECO:0000269|PubMed:30523278}.
CC -!- DOMAIN: The complex formed by AMN and CUBN is composed of a 400
CC Angstrom long stem and a globular crown region. The stem region is
CC probably formed by AMN and the CUBN N-terminal region, including the
CC EGF-like domains. The crown is probably formed by the CUBN CUB domains.
CC {ECO:0000269|PubMed:30523278}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9BXJ7}.
CC -!- PTM: A soluble form arises by proteolytic removal of the membrane
CC anchor. {ECO:0000250|UniProtKB:Q9BXJ7}.
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DR AlphaFoldDB; F1SAM7; -.
DR SMR; F1SAM7; -.
DR STRING; 9823.ENSSSCP00000002732; -.
DR PaxDb; F1SAM7; -.
DR HOGENOM; CLU_050471_0_0_1; -.
DR InParanoid; F1SAM7; -.
DR OrthoDB; 827066at2759; -.
DR TreeFam; TF323790; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR InterPro; IPR026112; AMN.
DR PANTHER; PTHR14995; PTHR14995; 1.
DR Pfam; PF14828; Amnionless; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Coated pit; Disulfide bond; Endosome; Glycoprotein;
KW Membrane; Protein transport; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000250|UniProtKB:Q9BXJ7"
FT CHAIN 20..519
FT /note="Protein amnionless"
FT /id="PRO_5013402183"
FT CHAIN 20..?
FT /note="Soluble protein amnionless"
FT /id="PRO_0000447653"
FT TOPO_DOM 20..430
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 452..519
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 256..308
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT REGION 67..143
FT /note="Interaction with CUBN"
FT /evidence="ECO:0000250|UniProtKB:Q9BXJ7"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..152
FT /evidence="ECO:0000250|UniProtKB:Q9BXJ7"
FT DISULFID 193..267
FT /evidence="ECO:0000250|UniProtKB:Q9BXJ7"
FT DISULFID 259..265
FT /evidence="ECO:0000250|UniProtKB:Q9BXJ7"
FT DISULFID 277..303
FT /evidence="ECO:0000250|UniProtKB:Q9BXJ7"
FT DISULFID 288..304
FT /evidence="ECO:0000250|UniProtKB:Q9BXJ7"
FT DISULFID 293..307
FT /evidence="ECO:0000250|UniProtKB:Q9BXJ7"
SQ SEQUENCE 519 AA; 55186 MW; 919B8ED5E22572D3 CRC64;
MGAPGRVLLW LQLCALTRAA YKLWVPNTYF DAADNWSQNQ TPCAGAAVKF PADKMVSVLV
REGHSISDME ELQDRKRENI HSFIHCSFID RASPPASPFR CPAARTGALL PVQSLQCTCI
LAHRPLLPLD GEFVLASGAG FSAQNTGSHL DCSAGASALF LDPDRFLWHD PRLWSAGDAG
RSLFSVDAER VPCRHDDAVF PSDASFRVGL GPGTVRVRSV RALGQTFTRD EDLAAFLASR
AGRLRFHGSG ALSVDPEACA DPSGCVCGNA EVQPWICAAL LQPLGGRCPQ AACQDALRPE
GQCCDLCGAI VSLTHGPAFD LERYRARLLH AFLALPQYQG LRMAMSKVPR QPHLHEASGA
KADTEIQVVL AETGPETGSA GRLARALLAD IAEHGEALGV LSATARESGP PVGGSSAAGL
NAPGARSDLM GGLVAALLLL LLVLLVAALL LRRAGRLRWS RRHEAASEPA GTPLGFRNPV
FYTADSVDPP PAPQPDVRSS SRSYFINPLY GEAEAEAEA
