Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

EMILIN-2

Gene

Emilin2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

May be responsible for anchoring smooth muscle cells to elastic fibers, and may be involved not only in the formation of the elastic fiber, but also in the processes that regulate vessel assembly. Has cell adhesive capacity. Major component of the cochlear basilar membrane (BM) which may contribute to the developmental assembly or function of the BM.

GO - Biological processi

Keywordsi

Biological processCell adhesion

Enzyme and pathway databases

ReactomeiR-MMU-2129379 Molecules associated with elastic fibres

Names & Taxonomyi

Protein namesi
Recommended name:
EMILIN-2
Alternative name(s):
Basilin
Elastin microfibril interface-located protein 2
Short name:
Elastin microfibril interfacer 2
Gene namesi
Name:Emilin2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:2389136 Emilin2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 33Sequence analysisAdd BLAST33
ChainiPRO_000000781834 – 1074EMILIN-2Add BLAST1041

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi51 ↔ 113PROSITE-ProRule annotation
Glycosylationi58N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi77 ↔ 84PROSITE-ProRule annotation
Disulfide bondi112 ↔ 121PROSITE-ProRule annotation
Glycosylationi463N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi514N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi586N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi615N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei636PhosphoserineCombined sources1
Glycosylationi744N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi995N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ8K482
MaxQBiQ8K482
PaxDbiQ8K482
PRIDEiQ8K482

PTM databases

iPTMnetiQ8K482
PhosphoSitePlusiQ8K482

Expressioni

Tissue specificityi

Highest levels are present in cochlea of P8 pups, followed by modest levels in adult heart and lung, and much lower levels in forebrain, brainstem, cerebellum and hypothalamus. Very low levels detected in muscle, liver, kidney and eye.

Developmental stagei

Low levels detected in cochlea in neonatal pups at P1. Levels increased 2-fold by P5 and rose further to 16-fold at P13. Expression declined somewhat in adult mice. At E9.5, as during all stages of development, it is strongly expressed in the neural fold, the limbbuds and the heart.1 Publication

Gene expression databases

BgeeiENSMUSG00000024053
CleanExiMM_EMILIN2
ExpressionAtlasiQ8K482 baseline and differential
GenevisibleiQ8K482 MM

Interactioni

Subunit structurei

Homotrimer associated through a moderately stable interaction of the C-terminal globular C1q domains, allowing the nucleation of the triple helix and then a further quaternary assembly to higher-order polymers via intermolecular disulfide bonds (By similarity). Interacts with EMILIN1.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ8K482
SMRiQ8K482
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini47 – 123EMIPROSITE-ProRule annotationAdd BLAST77
Domaini852 – 913Collagen-likeAdd BLAST62
Domaini922 – 1073C1qPROSITE-ProRule annotationAdd BLAST152

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili181 – 218Sequence analysisAdd BLAST38
Coiled coili259 – 345Sequence analysisAdd BLAST87
Coiled coili374 – 394Sequence analysisAdd BLAST21
Coiled coili533 – 554Sequence analysisAdd BLAST22
Coiled coili582 – 620Sequence analysisAdd BLAST39

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi783 – 851Pro-richAdd BLAST69
Compositional biasi914 – 924Pro-richAdd BLAST11

Keywords - Domaini

Coiled coil, Collagen, Signal

Phylogenomic databases

eggNOGiENOG410IFE8 Eukaryota
ENOG410ZUQR LUCA
GeneTreeiENSGT00660000095314
HOGENOMiHOG000060078
HOVERGENiHBG051474
InParanoidiQ8K482
OMAiQLEWRCC
OrthoDBiEOG091G0C3E
PhylomeDBiQ8K482
TreeFamiTF331033

Family and domain databases

Gene3Di2.60.120.40, 1 hit
InterProiView protein in InterPro
IPR001073 C1q_dom
IPR011489 EMI_domain
IPR008983 Tumour_necrosis_fac-like_dom
PfamiView protein in Pfam
PF00386 C1q, 1 hit
PF07546 EMI, 1 hit
SMARTiView protein in SMART
SM00110 C1Q, 1 hit
SUPFAMiSSF49842 SSF49842, 1 hit
PROSITEiView protein in PROSITE
PS50871 C1Q, 1 hit
PS51041 EMI, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8K482-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCQETPPRPR APSRWTPALL ALLALGGAGL CHASSQPGYH ARPSARNKNW
60 70 80 90 100
CAYIVNKNVS CTVQEGSESF IQAQYNCPWN QMPCPSALVY RVNFRPRFVT
110 120 130 140 150
RYKIVTQLEW RCCPGFRGPD CQEGPKDHMK TPRPPSARPK NNLKKATDTD
160 170 180 190 200
PSQVSQPKKT LSPTNAVEPG QVADAKQGPP ELQQSKVQVL EEKVVRLTRM
210 220 230 240 250
VLDLQSTVVG LKENLKHTIQ DDGRKEPDSW LGPLHPQPTP DSPLAGDAEP
260 270 280 290 300
SQLPGIPSSK ESGMKDIKSE LAEVKDTLKT KSDKLEELDG KVKGYEGQLK
310 320 330 340 350
QLQEAAQGPT VTMTTNELYQ AYVDSKIDAL REELMEGMDR KLADLKNTCE
360 370 380 390 400
YKLVGLQQQC DDYGSSYLGV IELIGEKEAS LKKDIADLRA QLQDPVAQPS
410 420 430 440 450
CCNGQKSSDF GPQIKALDQK IERVAEATRM LNGRLDNEFD RLSVPEPDAD
460 470 480 490 500
FDARWTELDA RINVTEKNAE EHCFYIEETL RGTINGEVDD LRKLLNEKIH
510 520 530 540 550
SLEDRLGIVL QAANSSDVEL TPMGPALPEQ PGAENEQVLM ELSRLKDKVQ
560 570 580 590 600
VVEDFCLQSL PHGIDGALPS VEDLTHVSLS LLESLNDTMH RQFQETSHSI
610 620 630 640 650
QKLQEDVNAL HSQLNHSECT GTYLQNGVSD SRTGDSMEAS GFTKTGEQER
660 670 680 690 700
TVGTVPSPGT PAAPCCGQLE ERWQKLQNQM LAELDTCKES AHGVQSGVSA
710 720 730 740 750
IEGRVFQLEQ TCRRLDTISG SLQRIKEGLG KHVGSLWNCI RQMNGTLKSH
760 770 780 790 800
SRDISGLKNS VQQFYSHVFQ ISTDLQDLVK FQPSATEEPS EATEGPSGKT
810 820 830 840 850
PLESTRPSEE APTEPPRLTP LPEDPAGPPQ TGQQPVLPQR PLQPPPLPAW
860 870 880 890 900
PGRTGLPFLP GSSGVIMETG EAGPPGRMGV SGRGLPRGVD GQMGQGPIHS
910 920 930 940 950
SEGYAGAPGY PKSPPVTTPG VPLPTLVSFS AGLTQKPFPS DGGVVLFNKV
960 970 980 990 1000
LVNDGDVYNP NTGIFTAPYD GRYLITATLT PERDTYVEAV LSVSNASVAQ
1010 1020 1030 1040 1050
LHTAGYRREF LEYHRPPGAV HTCGGPGAFH LIVHLKAGDG VNVVVTGGRL
1060 1070
AHTDFDEMYS TFSGVFLYPF LSHL
Length:1,074
Mass (Da):117,310
Last modified:October 1, 2002 - v1
Checksum:i4B81728C83CE52A7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF468645 mRNA Translation: AAM53532.1
BC053753 mRNA Translation: AAH53753.1
CCDSiCCDS37686.1
RefSeqiNP_660140.1, NM_145158.3
UniGeneiMm.23462

Genome annotation databases

EnsembliENSMUST00000024849; ENSMUSP00000024849; ENSMUSG00000024053
GeneIDi246707
KEGGimmu:246707
UCSCiuc008dme.1 mouse

Similar proteinsi

Entry informationi

Entry nameiEMIL2_MOUSE
AccessioniPrimary (citable) accession number: Q8K482
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 1, 2002
Last modified: May 23, 2018
This is version 120 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health