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Q9JLN5 (ERMAP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Erythroid membrane-associated protein
Gene names
Name:Ermap
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length566 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Possible role as a cell-adhesion or receptor molecule of erythroid cells.

Subcellular location

Cell membrane; Single-pass type I membrane protein. Cytoplasm Ref.1.

Tissue specificity

Expressed in spleen and bone marrow. Ref.1

Developmental stage

First detected at E.11. Expressed in fetal liver at E12.5 and E13.5. Ref.1

Post-translational modification

Glycosylated By similarity.

Sequence similarities

Belongs to the immunoglobulin superfamily. BTN/MOG family.

Contains 1 B30.2/SPRY domain.

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Sequence caution

The sequence AAF31162.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH63257.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAE23390.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9JLN5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9JLN5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     125-147: VWVGNSSREDNVTLQVAVLGSDP → EFPYTGAQNLHRTKKPLLPLMTN
     148-566: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9JLN5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     142-143: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 566537Erythroid membrane-associated protein
PRO_0000226089

Regions

Topological domain30 – 246217Extracellular Potential
Transmembrane247 – 26721Helical; Potential
Topological domain268 – 566299Cytoplasmic Potential
Domain30 – 139110Ig-like V-type
Domain311 – 509199B30.2/SPRY

Amino acid modifications

Glycosylation1351N-linked (GlcNAc...) Potential
Glycosylation2141N-linked (GlcNAc...) Potential
Disulfide bond47 ↔ 123 By similarity

Natural variations

Alternative sequence125 – 14723VWVGN…LGSDP → EFPYTGAQNLHRTKKPLLPL MTN in isoform 2.
VSP_017425
Alternative sequence142 – 1432Missing in isoform 3.
VSP_017426
Alternative sequence148 – 566419Missing in isoform 2.
VSP_017427

Experimental info

Sequence conflict911Y → S in AAF31162. Ref.1
Sequence conflict1801T → A in AAF31162. Ref.1
Sequence conflict2211N → I in AAF31162. Ref.1
Sequence conflict2871N → S in AAF31162. Ref.1
Sequence conflict3741L → P in AAF31162. Ref.1
Sequence conflict4621F → L in BAC25788. Ref.2
Sequence conflict5411S → C in AAF31162. Ref.1
Sequence conflict5541L → F in AAF31162. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 7, 2006. Version 2.
Checksum: 0017069E16D5D112

FASTA56663,512
        10         20         30         40         50         60 
MERPSPCGSW LVGCLFTIAV FQPPVQVLGD AGKVYIAPLR DTANLPCPLF LWPNMVLSEM 

        70         80         90        100        110        120 
RWYRPGHLPR TQAVHVFRDG QDRDEDLMPE YKGRTALVRD AHKESYILQI SNVRLEDRGL 

       130        140        150        160        170        180 
YQCQVWVGNS SREDNVTLQV AVLGSDPYIH VKGYDAGWIE LLCQSVGWFP KPWTEWRDTT 

       190        200        210        220        230        240 
GRALLSLSEV HSLDENGLFR TAVSSRIRDN ALGNVSCTIH NEALGQEKTT AMIIGAPERG 

       250        260        270        280        290        300 
SLSSPAVALS VVLPVLGLLI LLGIWLICKQ KKSKEKLLYE QAMEVENLLE DHAKEKGRLH 

       310        320        330        340        350        360 
KALKKLRSEL KLKRAAANAG WRRARLHFVA VTLDPDTAHP KLILSEDRRC VRLGDRKRPV 

       370        380        390        400        410        420 
PDNPERFDFV VSVLGSEYFT TGCHYWEVYV GEKTKWILGV CSESVSRKGK VTASPANGHW 

       430        440        450        460        470        480 
LVRQSRGNEY EALTSPQTSF RLKESPKCVG IFLDYEAGII SFYNVTDKSH IFTFTHSFSS 

       490        500        510        520        530        540 
PLRPFFEPCL HDEGKNTAPL IICTELQKSE ESIVPKQEGK DRANGDVSLK MNPSLLSPQG 

       550        560 
SELFLLNDTW PSNLGPALKG LKVPSL

« Hide

Isoform 2 [UniParc].

Checksum: D94BAFF1D0ED3D94
Show »

FASTA14716,910
Isoform 3 [UniParc].

Checksum: 5A46DF790035C6C3
Show »

FASTA56463,300

References

« Hide 'large scale' references
[1]"Ermap, a gene coding for a novel erythroid specific adhesion/receptor membrane protein."
Ye T.-Z., Gordon C.T., Lai Y.-H., Fujiwara Y., Peters L.L., Perkins A.C., Chui D.H.K.
Gene 242:337-345(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
Strain: C57BL/6J.
Tissue: Erythroid cell.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 323-566 (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Bone and Liver.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF153906 mRNA. Translation: AAF31162.1. Different initiation.
AK028170 mRNA. Translation: BAC25788.1.
AK137510 mRNA. Translation: BAE23390.1. Different initiation.
BC063257 mRNA. Translation: AAH63257.1. Different initiation.
IPIIPI00124515.
IPI00652740.
IPI00742326.
RefSeqNP_038876.2. NM_013848.2.
UniGeneMm.290753.

3D structure databases

ProteinModelPortalQ9JLN5.
SMRQ9JLN5. Positions 27-237, 324-503.
ModBaseSearch...

PTM databases

PhosphoSiteQ9JLN5.

Proteomic databases

PRIDEQ9JLN5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID27028.
KEGGmmu:27028.
UCSCuc008ulh.2. mouse.
uc012dke.1. mouse.

Organism-specific databases

CTD114625.
MGIMGI:1349816. Ermap.

Phylogenomic databases

eggNOGNOG320971.
HOGENOMHOG000197761.
HOVERGENHBG050747.
InParanoidQ9JLN5.
KOK06712.

Gene expression databases

ArrayExpressQ9JLN5.
BgeeQ9JLN5.
CleanExMM_ERMAP.
GenevestigatorQ9JLN5.
GermOnlineENSMUSG00000028644. Mus musculus.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR008985. ConA-like_lec_gl_sf.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013106. Ig_V-set.
IPR003596. Ig_V-set_subgr.
IPR006574. PRY.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
[Graphical view]
PfamPF00622. SPRY. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PRINTSPR01407. BUTYPHLNCDUF.
SMARTSM00406. IGv. 1 hit.
SM00589. PRY. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMSSF49899. ConA_like_lec_gl. 1 hit.
PROSITEPS50188. B302_SPRY. 1 hit.
PS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio304957.
SOURCESearch...

Entry information

Entry nameERMAP_MOUSE
AccessionPrimary (citable) accession number: Q9JLN5
Secondary accession number(s): Q3UV82, Q6P4T5, Q8CEH1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: March 7, 2006
Last modified: May 1, 2013
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents