GLPA_PANTR
ID GLPA_PANTR Reviewed; 149 AA.
AC Q28913; Q8WMM7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Glycophorin-A;
DE AltName: CD_antigen=CD235a;
DE Flags: Precursor;
GN Name=GYPA; Synonyms=GPA;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7563135; DOI=10.1007/bf00160319;
RA Huang C.-H., Xie S.S., Socha W., Blumenfeld O.O.;
RT "Sequence diversification and exon inactivation in the glycophorin A gene
RT family from chimpanzee to human.";
RL J. Mol. Evol. 41:478-486(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-144.
RA Baum J., Ward R.H., Conway D.J.;
RT "Molecular population genetic analysis of variation in Glycophorin A
RT (GYPA).";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glycophorin A is the major intrinsic membrane protein of the
CC erythrocyte. Appears to be important for the function of SLC4A1 and is
CC required for high activity of SLC4A1. May be involved in translocation
CC of SLC4A1 to the plasma membrane (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- SIMILARITY: Belongs to the glycophorin-A family. {ECO:0000305}.
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DR EMBL; S79724; AAB35338.1; -; mRNA.
DR EMBL; AJ309708; CAC83872.1; -; Genomic_DNA.
DR AlphaFoldDB; Q28913; -.
DR SMR; Q28913; -.
DR STRING; 9598.ENSPTRP00000028288; -.
DR PaxDb; Q28913; -.
DR eggNOG; ENOG502THAT; Eukaryota.
DR InParanoid; Q28913; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Sialic acid; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..149
FT /note="Glycophorin-A"
FT /id="PRO_0000012135"
FT TOPO_DOM 20..90
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 91..113
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 114..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 122..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02724"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02724"
FT CARBOHYD 21
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 22
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 23
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 29
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 30
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 31
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 32
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 35
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 37
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 40
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 43
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 44
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 51
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 55
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 62
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 68
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CONFLICT 114
FT /note="R -> C (in Ref. 2; CAC83872)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 149 AA; 16404 MW; 9AB52EC62FA34607 CRC64;
MYGKIIFVLL LSAIVSISAS STTEVAMHTS TSSVTKSYIS SETSDKHKWD TYPATPRAHE
VSEIYVTTVY PPEEENGEGV QLVHRFSEPE ITLIIFGVMA GVIGTILLIY YSIRRLIKKS
PSDVKPLPSP DTDVPLSSVE IENPETSDQ
