GLPA_PIG
ID GLPA_PIG Reviewed; 133 AA.
AC P02725;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Glycophorin-A;
DE AltName: CD_antigen=CD235a;
GN Name=GYPA;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE OF 1-43 AND 47-106.
RX PubMed=7462200; DOI=10.1093/oxfordjournals.jbchem.a133143;
RA Honma K., Tomita M., Hamada A.;
RT "Amino acid sequence and attachment sites of oligosaccharide units of
RT porcine erythrocyte glycophorin.";
RL J. Biochem. 88:1679-1691(1980).
RN [2]
RP PROTEIN SEQUENCE OF 36-54 AND 98-133.
RX PubMed=546438; DOI=10.1016/0005-2795(79)90211-3;
RA Honma K., Tomita M., Hamada A.;
RT "Partial amino acid sequence of glycophorin from porcine erythrocyte
RT membranes.";
RL Biochim. Biophys. Acta 580:210-215(1979).
CC -!- FUNCTION: Glycophorin A is the major intrinsic membrane
CC sialoglycoprotein of the erythrocyte. Appears to be important for the
CC function of SLC4A1 and is required for high activity of SLC4A1. May be
CC involved in translocation of SLC4A1 to the plasma membrane (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- SIMILARITY: Belongs to the glycophorin-A family. {ECO:0000305}.
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DR PIR; A91958; GFPGE.
DR AlphaFoldDB; P02725; -.
DR SMR; P02725; -.
DR iPTMnet; P02725; -.
DR PRIDE; P02725; -.
DR InParanoid; P02725; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR InterPro; IPR001195; Glycophorin.
DR InterPro; IPR018938; Glycophorin_CS.
DR PANTHER; PTHR13813; PTHR13813; 1.
DR PIRSF; PIRSF002466; Glycophorin; 1.
DR PROSITE; PS00312; GLYCOPHORIN_A; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Membrane; Reference proteome;
KW Sialic acid; Transmembrane; Transmembrane helix.
FT CHAIN 1..133
FT /note="Glycophorin-A"
FT /id="PRO_0000149049"
FT TOPO_DOM 1..62
FT /note="Extracellular"
FT TRANSMEM 63..85
FT /note="Helical"
FT TOPO_DOM 86..133
FT /note="Cytoplasmic"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 1
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7462200"
FT CARBOHYD 6
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7462200"
FT CARBOHYD 11
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:7462200"
FT CARBOHYD 13
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7462200"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7462200"
FT CARBOHYD 21
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7462200"
FT CARBOHYD 23
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7462200"
FT CARBOHYD 30
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7462200"
FT CARBOHYD 31
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:7462200"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7462200"
FT CARBOHYD 41
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7462200"
FT CARBOHYD 48
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7462200"
SQ SEQUENCE 133 AA; 14000 MW; 7B936EF93652547F CRC64;
TETPVTGEQG SATPGNVSNA TVTAGKPSAT SPGVMTIKNT TAVVQKETGV PESYHQDFSH
AEITGIIFAV MAGLLLIIFL IAYLIRRMIK KPLPVPKPQD SPDIGTENTA DPSELQDTED
PPLTSVEIET PAS