GLPC_HUMAN
ID GLPC_HUMAN Reviewed; 128 AA.
AC P04921; B2R522; Q53SV9; Q92642;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Glycophorin-C;
DE AltName: Full=Glycoconnectin;
DE AltName: Full=Glycophorin-D;
DE Short=GPD;
DE AltName: Full=Glycoprotein beta;
DE AltName: Full=PAS-2';
DE AltName: Full=Sialoglycoprotein D;
DE AltName: CD_antigen=CD236;
GN Name=GYPC; Synonyms=GLPC, GPC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GLYCOPHORIN-C).
RX PubMed=2416746; DOI=10.1016/s0021-9258(17)42458-6;
RA Colin Y., Rahuel C., London J., Romeo P.-H., D'Auriol L., Galibert F.,
RA Cartron J.-P.;
RT "Isolation of cDNA clones and complete amino acid sequence of human
RT erythrocyte glycophorin C.";
RL J. Biol. Chem. 261:229-233(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GLYCOPHORIN-C).
RX PubMed=3606576; DOI=10.1042/bj2430277;
RA High S., Tanner M.J.A.;
RT "Human erythrocyte membrane sialoglycoprotein beta. The cDNA sequence
RT suggests the absence of a cleaved N-terminal signal sequence.";
RL Biochem. J. 243:277-280(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GLYCOPHORIN-C).
RX PubMed=3544149; DOI=10.1016/s0338-4535(86)80020-4;
RA Cartron J.-P., Colin Y., le van Kim C., Rahuel C., Blanchard D., Bloy C.,
RA London J.;
RT "Structure of human erythrocyte glycophorin C deduced from cDNA analysis.";
RL Rev. Fr. Transfus. Immunohematol. 29:267-285(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GLYCOPHORIN-C).
RC TISSUE=Liver;
RX PubMed=3595602; DOI=10.1111/j.1432-1033.1987.tb11478.x;
RA le van Kim C., Colin Y., Blanchard D., Dahr W., London J., Cartron J.-P.;
RT "Gerbich blood group deficiency of the Ge:-1,-2,-3 and Ge:-1,-2,3 types.
RT Immunochemical study and genomic analysis with cDNA probes.";
RL Eur. J. Biochem. 165:571-579(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RC TISSUE=Spleen;
RX PubMed=2349119; DOI=10.1093/nar/18.10.3076;
RA le van Kim C., Mitjavila M.T., Clerget M., Cartron J.-P., Colin Y.;
RT "An ubiquitous isoform of glycophorin C is produced by alternative
RT splicing.";
RL Nucleic Acids Res. 18:3076-3076(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GLYCOPHORIN-C).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-124.
RG SeattleSNPs variation discovery resource;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GLYCOPHORIN-C).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 49-88.
RX PubMed=3571235; DOI=10.1016/s0021-9258(18)45646-3;
RA Blanchard D., Dahr W., Hummel M., Latron F., Beyreuther K., Cartron J.-P.;
RT "Glycophorins B and C from human erythrocyte membranes. Purification and
RT sequence analysis.";
RL J. Biol. Chem. 262:5808-5811(1987).
RN [11]
RP PROTEIN SEQUENCE OF 1-87.
RC TISSUE=Blood;
RA Dahr W., Humel M., Blanchard D., Beyreuther K., Cartron J.-P.;
RT "Isolation and structural analysis of glycophorin C.";
RL Biol. Chem. Hoppe-Seyler 366:777-778(1985).
RN [12]
RP PROTEIN SEQUENCE OF 1-48.
RC TISSUE=Blood;
RX PubMed=4074499; DOI=10.1515/bchm3.1985.366.2.1067;
RA Dahr W., Beyreuther K.;
RT "A revision of the N-terminal structure of sialoglycoprotein D (glycophorin
RT C) from human erythrocyte membranes.";
RL Biol. Chem. Hoppe-Seyler 366:1067-1070(1985).
RN [13]
RP PRELIMINARY PROTEIN SEQUENCE OF 1-48, AND GLYCOSYLATION AT SER-3; THR-4;
RP SER-6; ASN-8; SER-9; THR-10; SER-15; SER-24; SER-26; THR-27; THR-28;
RP THR-31; THR-32; THR-33 AND SER-42.
RC TISSUE=Blood;
RX PubMed=7106126; DOI=10.1111/j.1432-1033.1982.tb06650.x;
RA Dahr W., Beyreuther K., Kordowicz M., Krueger J.;
RT "N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from
RT human erythrocyte membranes.";
RL Eur. J. Biochem. 125:57-62(1982).
RN [14]
RP PROTEIN SEQUENCE OF 30-91.
RX PubMed=2776757; DOI=10.1111/j.1432-1033.1989.tb21093.x;
RA El-Maliki B., Blanchard D., Dahr W., Beyreuther K., Cartron J.-P.;
RT "Structural homology between glycophorins C and D of human erythrocytes.";
RL Eur. J. Biochem. 183:639-643(1989).
RN [15]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
RX PubMed=2584223; DOI=10.1016/s0021-9258(19)47077-4;
RA le van Kim C., Colin Y., Mitjavila M.T., Clerget M., Dubart A.,
RA Nakazawa M., Vainchenker W., Cartron J.-P.;
RT "Structure of the promoter region and tissue specificity of the human
RT glycophorin C gene.";
RL J. Biol. Chem. 264:20407-20414(1989).
RN [16]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-128.
RX PubMed=2818576; DOI=10.1042/bj2620047;
RA High S., Tanner M.J.A., Macdonald E.N., Anstee D.J.;
RT "Rearrangements of the red-cell membrane glycophorin C (sialoglycoprotein
RT beta) gene. A further study of alterations in the glycophorin C gene.";
RL Biochem. J. 262:47-54(1989).
RN [17]
RP GENE STRUCTURE.
RX PubMed=2917976; DOI=10.1016/s0021-9258(19)84916-5;
RA Colin Y., le van Kim C., Tsapis A., Clerget M., D'Auriol L., London J.,
RA Galibert F., Cartron J.-P.;
RT "Human erythrocyte glycophorin C. Gene structure and rearrangement in
RT genetic variants.";
RL J. Biol. Chem. 264:3773-3780(1989).
RN [18]
RP POLYMORPHISM, AND INVOLVEMENT IN PROTECTION AGAINST MALARIA.
RX PubMed=12469115; DOI=10.1038/nm807;
RA Maier A.G., Duraisingh M.T., Reeder J.C., Patel S.S., Kazura J.W.,
RA Zimmerman P.A., Cowman A.F.;
RT "Plasmodium falciparum erythrocyte invasion through glycophorin C and
RT selection for Gerbich negativity in human populations.";
RL Nat. Med. 9:87-92(2003).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [20]
RP GLYCOSYLATION AT SER-42, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 11:1-17(2012).
RN [21]
RP POLYMORPHISM, AND VARIANT SER-8.
RX PubMed=1991173;
RA Chang S., Reid M.E., Conboy J., Kan Y.W., Mohandas N.;
RT "Molecular characterization of erythrocyte glycophorin C variants.";
RL Blood 77:644-648(1991).
RN [22]
RP POLYMORPHISM, AND VARIANT PHE-14.
RX PubMed=1413665; DOI=10.1111/j.1423-0410.1992.tb01220.x;
RA King M.J., Avent N.D., Mallinson G., Reid M.E.;
RT "Point mutation in the glycophorin C gene results in the expression of the
RT blood group antigen Dha.";
RL Vox Sang. 63:56-58(1992).
RN [23]
RP POLYMORPHISM, AND VARIANT SER-23.
RX PubMed=8219208;
RA Daniels G., King M.J., Avent N.D., Khalid G., Reid M.E., Mallinson G.,
RA Symthe J., Cedergren B.;
RT "A point mutation in the GYPC gene results in the expression of the blood
RT group Ana antigen on glycophorin D but not on glycophorin C: further
RT evidence that glycophorin D is a product of the GYPC gene.";
RL Blood 82:3198-3203(1993).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: This protein is a minor sialoglycoprotein in human
CC erythrocyte membranes. The blood group Gerbich antigens and receptors
CC for Plasmodium falciparum merozoites are most likely located within the
CC extracellular domain. Glycophorin-C plays an important role in
CC regulating the stability of red cells.
CC -!- INTERACTION:
CC P04921; O95870: ABHD16A; NbExp=3; IntAct=EBI-7797098, EBI-348517;
CC P04921; Q13520: AQP6; NbExp=3; IntAct=EBI-7797098, EBI-13059134;
CC P04921; O15529: GPR42; NbExp=3; IntAct=EBI-7797098, EBI-18076404;
CC P04921; Q96GM1: PLPPR2; NbExp=3; IntAct=EBI-7797098, EBI-12955265;
CC P04921; Q8TEB9: RHBDD1; NbExp=3; IntAct=EBI-7797098, EBI-9916444;
CC P04921; Q3SXP7: SHISAL1; NbExp=3; IntAct=EBI-7797098, EBI-18037857;
CC P04921; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-7797098, EBI-18159983;
CC P04921; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-7797098, EBI-8638294;
CC P04921; Q6PEY1: TMEM88; NbExp=3; IntAct=EBI-7797098, EBI-17198826;
CC P04921; O95858: TSPAN15; NbExp=3; IntAct=EBI-7797098, EBI-7361096;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type III membrane
CC protein. Note=Linked to the membrane via band 4.1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Glycophorin-C;
CC IsoId=P04921-1; Sequence=Displayed;
CC Name=Glycophorin-D;
CC IsoId=P04921-2; Sequence=VSP_001777;
CC Name=3; Synonyms=IsoGPC;
CC IsoId=P04921-3; Sequence=VSP_054790;
CC -!- TISSUE SPECIFICITY: Glycophorin-C is expressed in erythrocytes.
CC Glycophorin-D and IsoGPC are ubiquitously expressed.
CC {ECO:0000269|PubMed:2349119}.
CC -!- PTM: O-glycosylated with core 1 or possibly core 8 glycans.
CC {ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:7106126}.
CC -!- POLYMORPHISM: GYPC is responsible for the Gerbich blood group system
CC (Ge) [MIM:616089]. Ge negative individuals carry a deletion of GYPC
CC exon 3. {ECO:0000269|PubMed:3595602}.
CC -!- POLYMORPHISM: Deletion of exon 3 in GYPC results in resistance to
CC Plasmodium falciparum invasion and protection against severe malaria
CC [MIM:611162]. {ECO:0000269|PubMed:12469115}.
CC -!- SIMILARITY: Belongs to the glycophorin-C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA32093.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation
CC database;
CC URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=gerbich";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Glycophorin C entry;
CC URL="https://en.wikipedia.org/wiki/Glycophorin_C";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/gypc/";
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DR EMBL; M11802; AAA60023.1; -; mRNA.
DR EMBL; M36284; AAA52625.1; -; mRNA.
DR EMBL; X12496; CAA31016.1; -; mRNA.
DR EMBL; M28335; AAA52574.1; -; mRNA.
DR EMBL; X51973; CAA36235.1; -; mRNA.
DR EMBL; AK312032; BAG34969.1; -; mRNA.
DR EMBL; AY838876; AAV80423.1; -; Genomic_DNA.
DR EMBL; AC013474; AAY14660.1; -; Genomic_DNA.
DR EMBL; BC106051; AAI06052.1; -; mRNA.
DR EMBL; BC104246; AAI04247.1; -; mRNA.
DR EMBL; BC104247; AAI04248.1; -; mRNA.
DR EMBL; X14242; CAA32458.1; -; Genomic_DNA.
DR EMBL; M29662; AAA52626.1; -; Genomic_DNA.
DR EMBL; X13890; CAA32093.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X13892; CAA32093.1; JOINED; Genomic_DNA.
DR EMBL; X13893; CAA32093.1; JOINED; Genomic_DNA.
DR CCDS; CCDS2136.1; -. [P04921-1]
DR CCDS; CCDS46402.1; -. [P04921-3]
DR CCDS; CCDS58724.1; -. [P04921-2]
DR PIR; A92573; GFHUC.
DR RefSeq; NP_001243513.1; NM_001256584.1. [P04921-2]
DR RefSeq; NP_002092.1; NM_002101.4. [P04921-1]
DR RefSeq; NP_058131.1; NM_016815.3. [P04921-3]
DR PDB; 2EJY; NMR; -; B=117-126.
DR PDBsum; 2EJY; -.
DR AlphaFoldDB; P04921; -.
DR SMR; P04921; -.
DR BioGRID; 109250; 14.
DR CORUM; P04921; -.
DR ELM; P04921; -.
DR IntAct; P04921; 12.
DR MINT; P04921; -.
DR STRING; 9606.ENSP00000259254; -.
DR GlyConnect; 189; 7 O-Linked glycans (1 site).
DR GlyGen; P04921; 16 sites, 14 O-linked glycans (5 sites).
DR iPTMnet; P04921; -.
DR PhosphoSitePlus; P04921; -.
DR BioMuta; GYPC; -.
DR DMDM; 121407; -.
DR EPD; P04921; -.
DR jPOST; P04921; -.
DR MassIVE; P04921; -.
DR MaxQB; P04921; -.
DR PaxDb; P04921; -.
DR PeptideAtlas; P04921; -.
DR PRIDE; P04921; -.
DR ProteomicsDB; 51759; -. [P04921-1]
DR ProteomicsDB; 51760; -. [P04921-2]
DR Antibodypedia; 2455; 489 antibodies from 34 providers.
DR DNASU; 2995; -.
DR Ensembl; ENST00000259254.9; ENSP00000259254.4; ENSG00000136732.16. [P04921-1]
DR Ensembl; ENST00000356887.12; ENSP00000349354.7; ENSG00000136732.16. [P04921-2]
DR Ensembl; ENST00000409836.3; ENSP00000386904.3; ENSG00000136732.16. [P04921-3]
DR GeneID; 2995; -.
DR KEGG; hsa:2995; -.
DR MANE-Select; ENST00000259254.9; ENSP00000259254.4; NM_002101.5; NP_002092.1.
DR UCSC; uc002tnq.5; human. [P04921-1]
DR CTD; 2995; -.
DR DisGeNET; 2995; -.
DR GeneCards; GYPC; -.
DR HGNC; HGNC:4704; GYPC.
DR HPA; ENSG00000136732; Tissue enhanced (bone).
DR MalaCards; GYPC; -.
DR MIM; 110750; gene.
DR MIM; 611162; phenotype.
DR MIM; 616089; phenotype.
DR neXtProt; NX_P04921; -.
DR OpenTargets; ENSG00000136732; -.
DR Orphanet; 288; Hereditary elliptocytosis.
DR PharmGKB; PA29082; -.
DR VEuPathDB; HostDB:ENSG00000136732; -.
DR eggNOG; ENOG502S5JS; Eukaryota.
DR GeneTree; ENSGT00510000049102; -.
DR HOGENOM; CLU_2183047_0_0_1; -.
DR InParanoid; P04921; -.
DR OMA; QPHGDVE; -.
DR OrthoDB; 1623675at2759; -.
DR PhylomeDB; P04921; -.
DR TreeFam; TF337016; -.
DR PathwayCommons; P04921; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR SignaLink; P04921; -.
DR SIGNOR; P04921; -.
DR BioGRID-ORCS; 2995; 9 hits in 1072 CRISPR screens.
DR ChiTaRS; GYPC; human.
DR EvolutionaryTrace; P04921; -.
DR GenomeRNAi; 2995; -.
DR Pharos; P04921; Tbio.
DR PRO; PR:P04921; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P04921; protein.
DR Bgee; ENSG00000136732; Expressed in blood and 184 other tissues.
DR Genevisible; P04921; HS.
DR GO; GO:0030863; C:cortical cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR InterPro; IPR001195; Glycophorin.
DR InterPro; IPR042192; Glycophorin-C.
DR InterPro; IPR003585; Neurexin-like.
DR PANTHER; PTHR47614; PTHR47614; 1.
DR PIRSF; PIRSF002466; Glycophorin; 1.
DR SMART; SM00294; 4.1m; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Blood group antigen; Cell membrane;
KW Direct protein sequencing; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Sialic acid; Transmembrane; Transmembrane helix.
FT CHAIN 1..128
FT /note="Glycophorin-C"
FT /id="PRO_0000149050"
FT TOPO_DOM 1..57
FT /note="Extracellular"
FT TRANSMEM 58..81
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT TOPO_DOM 82..128
FT /note="Cytoplasmic"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 8
FT /note="Not glycosylated; in variant Webb antigen"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 3
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:3571235,
FT ECO:0000269|PubMed:7106126"
FT CARBOHYD 4
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:3571235,
FT ECO:0000269|PubMed:7106126"
FT CARBOHYD 6
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:3571235,
FT ECO:0000269|PubMed:7106126"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7106126"
FT CARBOHYD 9
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:7106126"
FT CARBOHYD 10
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7106126"
FT CARBOHYD 15
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:3571235,
FT ECO:0000269|PubMed:7106126"
FT CARBOHYD 24
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:3571235,
FT ECO:0000269|PubMed:7106126"
FT CARBOHYD 26
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:3571235,
FT ECO:0000269|PubMed:7106126"
FT CARBOHYD 27
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:3571235,
FT ECO:0000269|PubMed:7106126"
FT CARBOHYD 28
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:3571235,
FT ECO:0000269|PubMed:7106126"
FT CARBOHYD 31
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:3571235,
FT ECO:0000269|PubMed:7106126"
FT CARBOHYD 32
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:3571235,
FT ECO:0000269|PubMed:7106126"
FT CARBOHYD 33
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:3571235,
FT ECO:0000269|PubMed:7106126"
FT CARBOHYD 42
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:22171320,
FT ECO:0000269|PubMed:3571235, ECO:0000269|PubMed:7106126"
FT VAR_SEQ 1..21
FT /note="Missing (in isoform Glycophorin-D)"
FT /evidence="ECO:0000305"
FT /id="VSP_001777"
FT VAR_SEQ 18..36
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:2349119"
FT /id="VSP_054790"
FT VARIANT 8
FT /note="N -> S (webb (WB) antigen; dbSNP:rs121912760)"
FT /evidence="ECO:0000269|PubMed:1991173"
FT /id="VAR_003193"
FT VARIANT 14
FT /note="L -> F (duch (DH(a)) antigen; dbSNP:rs121912761)"
FT /evidence="ECO:0000269|PubMed:1413665"
FT /id="VAR_003194"
FT VARIANT 23
FT /note="A -> S (ahonen (AN(a)) antigen; dbSNP:rs774359594)"
FT /evidence="ECO:0000269|PubMed:8219208"
FT /id="VAR_003195"
FT VARIANT 124
FT /note="K -> E (in dbSNP:rs28370000)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_021342"
SQ SEQUENCE 128 AA; 13811 MW; C9C654009A5642D5 CRC64;
MWSTRSPNST AWPLSLEPDP GMASASTTMH TTTIAEPDPG MSGWPDGRME TSTPTIMDIV
VIAGVIAAVA IVLVSLLFVM LRYMYRHKGT YHTNEAKGTE FAESADAALQ GDPALQDAGD
SSRKEYFI
