ERMAP_MOUSE
ID ERMAP_MOUSE Reviewed; 566 AA.
AC Q9JLN5; Q3UV82; Q6P4T5; Q8CEH1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Erythroid membrane-associated protein;
DE Flags: Precursor;
GN Name=Ermap;
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] (ISOFORM 1), DEVELOPMENTAL STAGE, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J; TISSUE=Erythroid cell;
RX PubMed=10721728; DOI=10.1016/s0378-1119(99)00516-8;
RA Ye T.-Z., Gordon C.T., Lai Y.-H., Fujiwara Y., Peters L.L., Perkins A.C.,
RA Chui D.H.K.;
RT "Ermap, a gene coding for a novel erythroid specific adhesion/receptor
RT membrane protein.";
RL Gene 242:337-345(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 323-566 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Bone, and Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: Possible role as a cell-adhesion or receptor molecule of
CC erythroid cells.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96PL5};
CC Single-pass type I membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000269|PubMed:10721728}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9JLN5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JLN5-2; Sequence=VSP_017425, VSP_017427;
CC Name=3;
CC IsoId=Q9JLN5-3; Sequence=VSP_017426;
CC -!- TISSUE SPECIFICITY: Expressed in spleen and bone marrow.
CC {ECO:0000269|PubMed:10721728}.
CC -!- DEVELOPMENTAL STAGE: First detected at 11 dpc. Expressed in fetal liver
CC at 12.5 dpc and 13.5 dpc. {ECO:0000269|PubMed:10721728}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF31162.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH63257.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE23390.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF153906; AAF31162.1; ALT_INIT; mRNA.
DR EMBL; AK028170; BAC25788.1; -; mRNA.
DR EMBL; AK137510; BAE23390.1; ALT_INIT; mRNA.
DR EMBL; BC063257; AAH63257.1; ALT_INIT; mRNA.
DR CCDS; CCDS18571.2; -. [Q9JLN5-1]
DR RefSeq; NP_038876.2; NM_013848.2. [Q9JLN5-1]
DR AlphaFoldDB; Q9JLN5; -.
DR SMR; Q9JLN5; -.
DR STRING; 10090.ENSMUSP00000123426; -.
DR GlyGen; Q9JLN5; 2 sites.
DR iPTMnet; Q9JLN5; -.
DR PhosphoSitePlus; Q9JLN5; -.
DR PaxDb; Q9JLN5; -.
DR PRIDE; Q9JLN5; -.
DR ProteomicsDB; 275645; -. [Q9JLN5-1]
DR ProteomicsDB; 275646; -. [Q9JLN5-2]
DR ProteomicsDB; 275647; -. [Q9JLN5-3]
DR Antibodypedia; 18175; 324 antibodies from 28 providers.
DR DNASU; 27028; -.
DR Ensembl; ENSMUST00000239029; ENSMUSP00000159033; ENSMUSG00000028644. [Q9JLN5-1]
DR GeneID; 27028; -.
DR KEGG; mmu:27028; -.
DR UCSC; uc008ulh.2; mouse. [Q9JLN5-2]
DR UCSC; uc012dke.1; mouse. [Q9JLN5-3]
DR CTD; 114625; -.
DR MGI; MGI:1349816; Ermap.
DR VEuPathDB; HostDB:ENSMUSG00000028644; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160531; -.
DR InParanoid; Q9JLN5; -.
DR OMA; QVMEVEN; -.
DR OrthoDB; 522383at2759; -.
DR BioGRID-ORCS; 27028; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Ermap; mouse.
DR PRO; PR:Q9JLN5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9JLN5; protein.
DR Bgee; ENSMUSG00000028644; Expressed in fetal liver hematopoietic progenitor cell and 74 other tissues.
DR ExpressionAtlas; Q9JLN5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF07686; V-set; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..566
FT /note="Erythroid membrane-associated protein"
FT /id="PRO_0000226089"
FT TOPO_DOM 30..246
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..566
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..139
FT /note="Ig-like V-type"
FT DOMAIN 311..509
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 125..147
FT /note="VWVGNSSREDNVTLQVAVLGSDP -> EFPYTGAQNLHRTKKPLLPLMTN
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017425"
FT VAR_SEQ 142..143
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017426"
FT VAR_SEQ 148..566
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017427"
FT CONFLICT 91
FT /note="Y -> S (in Ref. 1; AAF31162)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="T -> A (in Ref. 1; AAF31162)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="N -> I (in Ref. 1; AAF31162)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="N -> S (in Ref. 1; AAF31162)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="L -> P (in Ref. 1; AAF31162)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="F -> L (in Ref. 2; BAC25788)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="S -> C (in Ref. 1; AAF31162)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="L -> F (in Ref. 1; AAF31162)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 566 AA; 63512 MW; 0017069E16D5D112 CRC64;
MERPSPCGSW LVGCLFTIAV FQPPVQVLGD AGKVYIAPLR DTANLPCPLF LWPNMVLSEM
RWYRPGHLPR TQAVHVFRDG QDRDEDLMPE YKGRTALVRD AHKESYILQI SNVRLEDRGL
YQCQVWVGNS SREDNVTLQV AVLGSDPYIH VKGYDAGWIE LLCQSVGWFP KPWTEWRDTT
GRALLSLSEV HSLDENGLFR TAVSSRIRDN ALGNVSCTIH NEALGQEKTT AMIIGAPERG
SLSSPAVALS VVLPVLGLLI LLGIWLICKQ KKSKEKLLYE QAMEVENLLE DHAKEKGRLH
KALKKLRSEL KLKRAAANAG WRRARLHFVA VTLDPDTAHP KLILSEDRRC VRLGDRKRPV
PDNPERFDFV VSVLGSEYFT TGCHYWEVYV GEKTKWILGV CSESVSRKGK VTASPANGHW
LVRQSRGNEY EALTSPQTSF RLKESPKCVG IFLDYEAGII SFYNVTDKSH IFTFTHSFSS
PLRPFFEPCL HDEGKNTAPL IICTELQKSE ESIVPKQEGK DRANGDVSLK MNPSLLSPQG
SELFLLNDTW PSNLGPALKG LKVPSL
