GLPA_MOUSE
ID GLPA_MOUSE Reviewed; 168 AA.
AC P14220;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Glycophorin-A;
DE AltName: CD_antigen=CD235a;
GN Name=Gypa;
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 [MRNA], AND PROTEIN SEQUENCE OF 138-146.
RC STRAIN=BALB/cJ;
RX PubMed=2753361; DOI=10.1016/0378-1119(89)90080-2;
RA Matsui Y., Natori S., Obinata M.;
RT "Isolation of the cDNA clone for mouse glycophorin, erythroid-specific
RT membrane protein.";
RL Gene 77:325-332(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RX PubMed=2043106; DOI=10.1016/0006-291x(91)91968-i;
RA Gu H., Planas J., Gomez R., Wilson D.J.;
RT "Full length mouse glycophorin gene constructed using recombinant
RT polymerase chain reaction.";
RL Biochem. Biophys. Res. Commun. 177:202-208(1991).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=12940824; DOI=10.1046/j.1365-2443.2003.00674.x;
RA Arimitsu N., Akimitsu N., Kotani N., Takasaki S., Kina T., Hamamoto H.,
RA Kamura K., Sekimizu K.;
RT "Glycophorin A requirement for expression of O-linked antigens on the
RT erythrocyte membrane.";
RL Genes Cells 8:769-777(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-160 AND SER-166, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 III membrane protein.
CC -!- PTM: The N-terminal extracellular domain is heavily glycosylated on
CC serine and threonine residues. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: The amount of O-linked oligosaccharide chains in
CC the erythrocyte membrane decreases to 60% compared to that of the wild-
CC type mice. Erythrocytes lacking GPA are more sensitive to hypo-osmotic
CC stress. {ECO:0000269|PubMed:12940824}.
CC -!- SIMILARITY: Belongs to the glycophorin-A family. {ECO:0000305}.
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DR EMBL; M26385; AAA37709.1; -; mRNA.
DR EMBL; M73815; AAA37708.1; -; Genomic_DNA.
DR CCDS; CCDS40399.1; -.
DR PIR; JN0073; JN0073.
DR RefSeq; NP_034499.3; NM_010369.3.
DR AlphaFoldDB; P14220; -.
DR SMR; P14220; -.
DR STRING; 10090.ENSMUSP00000070836; -.
DR GlyConnect; 186; 5 N-Linked glycans, 4 O-Linked glycans.
DR GlyGen; P14220; 1 site, 9 N-linked glycans (1 site), 6 O-linked glycans (1 site).
DR iPTMnet; P14220; -.
DR PhosphoSitePlus; P14220; -.
DR PaxDb; P14220; -.
DR PeptideAtlas; P14220; -.
DR PRIDE; P14220; -.
DR ProteomicsDB; 267634; -.
DR DNASU; 14934; -.
DR Ensembl; ENSMUST00000063359; ENSMUSP00000070836; ENSMUSG00000051839.
DR GeneID; 14934; -.
DR KEGG; mmu:14934; -.
DR UCSC; uc009miz.1; mouse.
DR CTD; 2993; -.
DR MGI; MGI:95880; Gypa.
DR VEuPathDB; HostDB:ENSMUSG00000051839; -.
DR eggNOG; ENOG502THAT; Eukaryota.
DR GeneTree; ENSGT00550000075214; -.
DR HOGENOM; CLU_1585936_0_0_1; -.
DR InParanoid; P14220; -.
DR OMA; SYCISRM; -.
DR OrthoDB; 1500024at2759; -.
DR TreeFam; TF338555; -.
DR BioGRID-ORCS; 14934; 2 hits in 71 CRISPR screens.
DR PRO; PR:P14220; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P14220; protein.
DR Bgee; ENSMUSG00000051839; Expressed in fetal liver hematopoietic progenitor cell and 85 other tissues.
DR ExpressionAtlas; P14220; baseline and differential.
DR Genevisible; P14220; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0047484; P:regulation of response to osmotic stress; IMP:MGI.
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; Phosphoprotein;
KW Reference proteome; Sialic acid; Transmembrane; Transmembrane helix.
FT CHAIN 1..168
FT /note="Glycophorin-A"
FT /id="PRO_0000149048"
FT TOPO_DOM 1..108
FT /note="Extracellular"
FT TRANSMEM 109..131
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT TOPO_DOM 132..168
FT /note="Cytoplasmic"
FT REGION 139..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02724"
FT MOD_RES 160
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02724"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 61..100
FT /note="ATMSTPAIHVSTYHTAPTEVSAAFEEQPVSPHIGGMPSPI -> SAAFEEQP
FT VSPHIGGMPSPIATMSTPAIHVSTYHTAPTEV (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 168 AA; 17664 MW; 2DF15DDA3A587EC6 CRC64;
MTESTAAVTT SGHSLTTTFH IPSSQHYQEE HSPSLSGSDS LLQITTPVVA STVGNPNQHS
ATMSTPAIHV STYHTAPTEV SAAFEEQPVS PHIGGMPSPI QHDFPALVMI LIILGVMAGI
IGTILLISYC ISRMTKKSSV DIQSPEGGDN SVPLSSIEQT PNEESSNV
