MDGA2_HUMAN
ID MDGA2_HUMAN Reviewed; 956 AA.
AC Q7Z553; F6W3S7; J3KPX6;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=MAM domain-containing glycosylphosphatidylinositol anchor protein 2;
DE AltName: Full=MAM domain-containing protein 1;
DE Flags: Precursor;
GN Name=MDGA2; Synonyms=MAMDC1; ORFNames=UNQ8188/PRO23197;
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 1).
RA Huang C.Q., Wu S.L., Liu S.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Thalamus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-956 (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 335-956 (ISOFORMS 1/2).
RA Shan Y.X., Yu L.;
RT "Cloning and characterization of a novel human MAMDC1 gene.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=19997561; DOI=10.1371/journal.pone.0008037;
RA Hellquist A., Zucchelli M., Lindgren C.M., Saarialho-Kere U.,
RA Jaervinen T.M., Koskenmies S., Julkunen H., Onkamo P., Skoog T.,
RA Panelius J., Raeisanen-Sokolowski A., Hasan T., Widen E., Gunnarson I.,
RA Svenungsson E., Padyukov L., Assadi G., Berglind L., Maekelae V.V.,
RA Kivinen K., Wong A., Cunningham Graham D.S., Vyse T.J., D'Amato M.,
RA Kere J.;
RT "Identification of MAMDC1 as a candidate susceptibility gene for systemic
RT lupus erythematosus (SLE).";
RL PLoS ONE 4:E8037-E8037(2009).
CC -!- FUNCTION: May be involved in cell-cell interactions. {ECO:0000250}.
CC -!- SUBUNIT: Interacts (through the Ig-like domains) with NLGN2.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7Z553-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z553-2; Sequence=VSP_042468;
CC Name=3;
CC IsoId=Q7Z553-3; Sequence=VSP_045240;
CC -!- TISSUE SPECIFICITY: Detected in Leydig cells, syncytiotrophoblast,
CC duodenal villi epithelial cells and neutrophils from kidney and
CC cutaneous squamous cell carcinoma (at protein level).
CC {ECO:0000269|PubMed:19997561}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP97010.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY369208; AAQ73312.1; -; mRNA.
DR EMBL; AY358125; AAQ88492.1; -; mRNA.
DR EMBL; AK309211; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL079306; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL157792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL162551; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL358832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY328482; AAP97010.1; ALT_INIT; mRNA.
DR CCDS; CCDS41948.1; -. [Q7Z553-2]
DR CCDS; CCDS45098.3; -. [Q7Z553-3]
DR RefSeq; NP_001106970.3; NM_001113498.2. [Q7Z553-1]
DR RefSeq; NP_878250.2; NM_182830.4. [Q7Z553-2]
DR RefSeq; XP_016876549.1; XM_017021060.1.
DR AlphaFoldDB; Q7Z553; -.
DR SMR; Q7Z553; -.
DR BioGRID; 127785; 2.
DR STRING; 9606.ENSP00000382178; -.
DR GlyGen; Q7Z553; 8 sites.
DR iPTMnet; Q7Z553; -.
DR PhosphoSitePlus; Q7Z553; -.
DR BioMuta; MDGA2; -.
DR DMDM; 46403175; -.
DR jPOST; Q7Z553; -.
DR MassIVE; Q7Z553; -.
DR PaxDb; Q7Z553; -.
DR PeptideAtlas; Q7Z553; -.
DR PRIDE; Q7Z553; -.
DR ProteomicsDB; 69257; -. [Q7Z553-1]
DR ProteomicsDB; 69258; -. [Q7Z553-2]
DR Antibodypedia; 162; 94 antibodies from 17 providers.
DR DNASU; 161357; -.
DR Ensembl; ENST00000357362.7; ENSP00000349925.3; ENSG00000139915.21. [Q7Z553-2]
DR Ensembl; ENST00000399232.8; ENSP00000382178.4; ENSG00000139915.21. [Q7Z553-3]
DR GeneID; 161357; -.
DR KEGG; hsa:161357; -.
DR MANE-Select; ENST00000399232.8; ENSP00000382178.4; NM_001113498.3; NP_001106970.4. [Q7Z553-3]
DR UCSC; uc001wwj.6; human. [Q7Z553-1]
DR CTD; 161357; -.
DR DisGeNET; 161357; -.
DR GeneCards; MDGA2; -.
DR HGNC; HGNC:19835; MDGA2.
DR HPA; ENSG00000139915; Group enriched (brain, retina, testis).
DR MIM; 611128; gene.
DR neXtProt; NX_Q7Z553; -.
DR OpenTargets; ENSG00000139915; -.
DR PharmGKB; PA162395090; -.
DR VEuPathDB; HostDB:ENSG00000139915; -.
DR eggNOG; ENOG502QSMD; Eukaryota.
DR GeneTree; ENSGT00940000155369; -.
DR HOGENOM; CLU_014908_0_0_1; -.
DR InParanoid; Q7Z553; -.
DR OMA; HKDETEY; -.
DR OrthoDB; 118847at2759; -.
DR PhylomeDB; Q7Z553; -.
DR TreeFam; TF330345; -.
DR PathwayCommons; Q7Z553; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR SIGNOR; Q7Z553; -.
DR BioGRID-ORCS; 161357; 15 hits in 1062 CRISPR screens.
DR ChiTaRS; MDGA2; human.
DR GenomeRNAi; 161357; -.
DR Pharos; Q7Z553; Tbio.
DR PRO; PR:Q7Z553; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q7Z553; protein.
DR Bgee; ENSG00000139915; Expressed in cortical plate and 71 other tissues.
DR ExpressionAtlas; Q7Z553; baseline and differential.
DR Genevisible; Q7Z553; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0021522; P:spinal cord motor neuron differentiation; ISS:HGNC-UCL.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.40.10; -; 7.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR000998; MAM_dom.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00629; MAM; 1.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SMART; SM00137; MAM; 1.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 6.
DR PROSITE; PS50060; MAM_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..931
FT /note="MAM domain-containing glycosylphosphatidylinositol
FT anchor protein 2"
FT /id="PRO_0000014859"
FT PROPEP 932..956
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000292043"
FT DOMAIN 27..127
FT /note="Ig-like 1"
FT DOMAIN 134..232
FT /note="Ig-like 2"
FT DOMAIN 242..328
FT /note="Ig-like 3"
FT DOMAIN 340..436
FT /note="Ig-like 4"
FT DOMAIN 442..533
FT /note="Ig-like 5"
FT DOMAIN 540..627
FT /note="Ig-like 6"
FT DOMAIN 638..739
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 746..921
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT LIPID 931
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 610
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 703
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 159..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 264..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 359..417
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 465..515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 561..611
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..229
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042468"
FT VAR_SEQ 1
FT /note="M -> MSVWSAGLLRSARRRRRGRTDGRRFLLRRAVPGHLGLARARVERAWL
FT AAGLLKVPLRTPWAGYVHVHVKM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045240"
FT VARIANT 608
FT /note="V -> F (in dbSNP:rs12590500)"
FT /id="VAR_059400"
FT CONFLICT 19..24
FT /note="SGQGVY -> EHLVIQ (in Ref. 3; AAQ88492)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="Missing (in Ref. 3; AAQ88492)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="E -> Q (in Ref. 2; AK309211)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="R -> K (in Ref. 2; AK309211)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="N -> S (in Ref. 2; AK309211)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="D -> N (in Ref. 3; AAQ88492)"
FT /evidence="ECO:0000305"
FT CONFLICT 930
FT /note="V -> I (in Ref. 2; AK309211)"
FT /evidence="ECO:0000305"
FT CONFLICT Q7Z553-3:50
FT /note="G -> S (in Ref. 2; AK309211)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 956 AA; 107436 MW; 6B70534BD35489B9 CRC64;
MDLLYGLVWL LTVLLEGISG QGVYAPPTVR IVHSGLACNI EEERYSERVY TIREGETLEL
TCLVTGHPRP QIRWTKTAGS ASDRFQDSSV FNETLRITNI QRHQGGRYYC KAENGLGSPA
IKSIRVDVYY LDDPVVTVHQ SIGEAKEQFY YERTVFLRCV ANSNPPVRYS WRRGQEVLLQ
GSDKGVEIYE PFFTQGETKI LKLKNLRPQD YANYSCIASV RNVCNIPDKM VSFRLSNKTA
SPSIKLLVDD PIVVNPGEAI TLVCVTTGGE PAPSLTWVRS FGTLPEKTVL NGGTLTIPAI
TSDDAGTYSC IANNNVGNPA KKSTNIIVRA LKKGRFWITP DPYHKDDNIQ IGREVKISCQ
VEAVPSEELT FSWFKNGRPL RSSERMVITQ TDPDVSPGTT NLDIIDLKFT DFGTYTCVAS
LKGGGISDIS IDVNISSSTV PPNLTVPQEK SPLVTREGDT IELQCQVTGK PKPIILWSRA
DKEVAMPDGS MQMESYDGTL RIVNVSREMS GMYRCQTSQY NGFNVKPREA LVQLIVQYPP
AVEPAFLEIR QGQDRSVTMS CRVLRAYPIR VLTYEWRLGN KLLRTGQFDS QEYTEYAVKS
LSNENYGVYN CSIINEAGAG RCSFLVTGKA YAPEFYYDTY NPVWQNRHRV YSYSLQWTQM
NPDAVDRIVA YRLGIRQAGQ QRWWEQEIKI NGNIQKGELI TYNLTELIKP EAYEVRLTPL
TKFGEGDSTI RVIKYSAPVN PHLREFHCGF EDGNICLFTQ DDTDNFDWTK QSTATRNTKY
TPNTGPNADR SGSKEGFYMY IETSRPRLEG EKARLLSPVF SIAPKNPYGP TNTAYCFSFF
YHMYGQHIGV LNVYLRLKGQ TTIENPLWSS SGNKGQRWNE AHVNIYPITS FQLIFEGIRG
PGIEGDIAID DVSIAEGECA KQDLATKNSV DGAVGILVHI WLFPIIVLIS ILSPRR
