ID   GLPA_CANLF              Reviewed;         129 AA.
AC   P02727; A7VLI4;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 3.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Glycophorin-A;
DE   AltName: CD_antigen=CD235a;
DE   Flags: Precursor;
GN   Name=GYPA;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=18380152;
RA   Sato K., Otsuka Y., Arashiki N., Komatsu T., Chen-Chi W., Tamahara S.,
RA   Inaba M.;
RT   "Identification of genes for two major sialoglycoproteins, glycophorin A
RT   and glycophorin C in canine red cell membranes.";
RL   Jpn. J. Vet. Res. 55:103-114(2008).
RN   [2]
RP   PROTEIN SEQUENCE OF 18-69, PYROGLUTAMATE FORMATION AT GLN-18, VARIANT
RP   PRO-31, AND GLYCOSYLATION AT SER-29; SER-30; THR-34; SER-40; THR-41; THR-48
RP   AND SER-56.
RX   PubMed=6838883; DOI=10.1016/0167-4838(83)90264-9;
RA   Murayama J., Yamashita T., Tomita M., Hamada A.;
RT   "Amino acid sequence and oligosaccharide attachment sites of the
RT   glycosylated domain of dog erythrocyte glycophorin.";
RL   Biochim. Biophys. Acta 742:477-483(1983).
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   EMBL; AB299408; BAF79931.1; -; mRNA.
DR   PIR; A05273; A05273.
DR   RefSeq; NP_001103430.1; NM_001109960.1.
DR   AlphaFoldDB; P02727; -.
DR   SMR; P02727; -.
DR   GlyConnect; 185; 3 O-Linked glycans.
DR   iPTMnet; P02727; -.
DR   PaxDb; P02727; -.
DR   Ensembl; ENSCAFT00040042095; ENSCAFP00040036715; ENSCAFG00040022681.
DR   Ensembl; ENSCAFT00845020235; ENSCAFP00845015862; ENSCAFG00845011416.
DR   GeneID; 100126181; -.
DR   KEGG; cfa:100126181; -.
DR   CTD; 2993; -.
DR   VEuPathDB; HostDB:ENSCAFG00845011416; -.
DR   eggNOG; ENOG502TE08; Eukaryota.
DR   GeneTree; ENSGT00550000075214; -.
DR   HOGENOM; CLU_154690_2_0_1; -.
DR   InParanoid; P02727; -.
DR   OMA; MYEKIVI; -.
DR   OrthoDB; 1548637at2759; -.
DR   Proteomes; UP000002254; Chromosome 15.
DR   Bgee; ENSCAFG00000031944; Expressed in bone marrow and 9 other tissues.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   InterPro; IPR001195; Glycophorin.
DR   PANTHER; PTHR13813; PTHR13813; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Membrane;
KW   Pyrrolidone carboxylic acid; Reference proteome; Sialic acid; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:6838883"
FT   CHAIN           18..129
FT                   /note="Glycophorin-A"
FT                   /id="PRO_0000149045"
FT   TOPO_DOM        18..82
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        104..129
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         18
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:6838883"
FT   CARBOHYD        29
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:6838883"
FT   CARBOHYD        30
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:6838883"
FT   CARBOHYD        34
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:6838883"
FT   CARBOHYD        40
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:6838883"
FT   CARBOHYD        41
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:6838883"
FT   CARBOHYD        48
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:6838883"
FT   CARBOHYD        56
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:6838883"
FT   VARIANT         31
FT                   /note="K -> P"
FT                   /evidence="ECO:0000269|PubMed:6838883"
FT   CONFLICT        27
FT                   /note="E -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        53
FT                   /note="Q -> E (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   129 AA;  14052 MW;  0F7EDA83CF212052 CRC64;
     MYEKIVIVLL LSGYISTQDV TEIIPHEISS KLPTQAGFIS TEDPSFNTPS TRQDPSGTMY
     QHLPDGGQKA RQQLVHIFSE PVIIGIIYAV MLGIIITILS IAFCIGQLTK KSSLPAQVAS
     PEDVDPEVL