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Protein

Multimerin-1

Gene

MMRN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Carrier protein for platelet (but not plasma) factor V/Va. Plays a role in the storage and stabilization of factor V in platelets. Upon release following platelet activation, may limit platelet and plasma factor Va-dependent thrombin generation. Ligand for integrin alpha-IIb/beta-3 and integrin alpha-V/beta-3 on activated platelets, and may function as an extracellular matrix or adhesive protein.3 Publications

GO - Molecular functioni

GO - Biological processi

  • blood coagulation Source: ProtInc
  • cell adhesion Source: ProtInc
  • platelet degranulation Source: Reactome

Enzyme and pathway databases

ReactomeiR-HSA-114608. Platelet degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Multimerin-1
Alternative name(s):
EMILIN-4
Elastin microfibril interface located protein 4
Short name:
Elastin microfibril interfacer 4
Endothelial cell multimerin
Cleaved into the following 2 chains:
Gene namesi
Name:MMRN1
Synonyms:ECM, EMILIN4, GPIA*, MMRN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiHostDB:ENSG00000138722.9.
HGNCiHGNC:7178. MMRN1.

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

Secreted

Pathology & Biotechi

Involvement in diseasei

Deficiency in multimerin-1 due to proteolytic degradation within the platelet alpha granules is associated with an autosomal dominant bleeding disorder (factor V Quebec).1 Publication

Organism-specific databases

DisGeNETi22915.
OpenTargetsiENSG00000138722.
PharmGKBiPA30891.

Polymorphism and mutation databases

BioMutaiMMRN1.
DMDMi143811421.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000000782120 – 1228Multimerin-1Add BLAST1209
ChainiPRO_0000367047184 – 1228Platelet glycoprotein Ia*Add BLAST1045
ChainiPRO_0000367048318 – 1228155 kDa platelet multimerinAdd BLAST911

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi21N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi97N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi114N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi120N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi136N-linked (GlcNAc...) (complex) asparagine2 Publications1
Disulfide bondi211 ↔ 272By similarity
Disulfide bondi238 ↔ 245By similarity
Disulfide bondi271 ↔ 280By similarity
Glycosylationi344N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi431N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi507N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi541N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi576N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi618N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi680N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi729N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi783N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi816N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi828N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi840N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi921N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi933N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi942N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi981N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1020N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi1045 ↔ 1056By similarity
Disulfide bondi1050 ↔ 1065By similarity
Disulfide bondi1067 ↔ 1076By similarity
Glycosylationi1075N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

The N-terminus is blocked.
Extensively N-glycosylated.4 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ13201.
MaxQBiQ13201.
PaxDbiQ13201.
PeptideAtlasiQ13201.
PRIDEiQ13201.

2D gel databases

OGPiQ13201.

PTM databases

iPTMnetiQ13201.
PhosphoSitePlusiQ13201.
UniCarbKBiQ13201.

Expressioni

Tissue specificityi

Synthesized by endothelial cells and megakaryocytes. Stored in platelet alpha granules and endothelial cell Weibel-Palade bodies, following activation of these cells, it is released and attached to megakaryocytes, platelets, endothelium and subendothelium of blood vessels. Not found in plasma. Found in vascular tissues such as placenta, lung, and liver.2 Publications

Gene expression databases

BgeeiENSG00000138722.
CleanExiHS_MMRN1.
ExpressionAtlasiQ13201. baseline and differential.
GenevisibleiQ13201. HS.

Organism-specific databases

HPAiHPA035769.

Interactioni

Subunit structurei

Multimeric. Composed of varying sized, disulfide-linked multimers, the smallest of which is a homotrimer. Proteolysis of the promultimerin in the N-terminal region, leads to the mature p155 form that is stored in platelets. Interacts with factor V/Va.3 Publications

Protein-protein interaction databases

BioGridi116577. 18 interactors.
IntActiQ13201. 3 interactors.
STRINGi9606.ENSP00000264790.

Structurei

3D structure databases

ProteinModelPortaliQ13201.
SMRiQ13201.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini207 – 282EMIPROSITE-ProRule annotationAdd BLAST76
Domaini1041 – 1077EGF-likePROSITE-ProRule annotationAdd BLAST37
Domaini1096 – 1228C1qPROSITE-ProRule annotationAdd BLAST133

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili333 – 365Sequence analysisAdd BLAST33
Coiled coili400 – 430Sequence analysisAdd BLAST31
Coiled coili503 – 523Sequence analysisAdd BLAST21
Coiled coili580 – 650Sequence analysisAdd BLAST71
Coiled coili675 – 726Sequence analysisAdd BLAST52
Coiled coili819 – 869Sequence analysisAdd BLAST51

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi186 – 188Cell attachment siteSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi189 – 192Poly-Ser4
Compositional biasi309 – 313Poly-Gln5

Keywords - Domaini

Coiled coil, EGF-like domain, Signal

Phylogenomic databases

eggNOGiENOG410IEM1. Eukaryota.
ENOG411182X. LUCA.
GeneTreeiENSGT00660000095560.
HOGENOMiHOG000113610.
HOVERGENiHBG108139.
InParanoidiQ13201.
OMAiCACRHPF.
OrthoDBiEOG091G00VO.
PhylomeDBiQ13201.
TreeFamiTF336041.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiView protein in InterPro
IPR001073. C1q_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR011489. EMI_domain.
IPR033188. MMRN1.
IPR008983. Tumour_necrosis_fac-like_dom.
PANTHERiPTHR15427:SF15. PTHR15427:SF15. 1 hit.
PfamiView protein in Pfam
PF00386. C1q. 1 hit.
PF00008. EGF. 1 hit.
PF07546. EMI. 1 hit.
PRINTSiPR00007. COMPLEMNTC1Q.
SMARTiView protein in SMART
SM00110. C1Q. 1 hit.
SM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiView protein in PROSITE
PS50871. C1Q. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS51041. EMI. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q13201-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MKGARLFVLL SSLWSGGIGL NNSKHSWTIP EDGNSQKTMP SASVPPNKIQ
60 70 80 90 100
SLQILPTTRV MSAEIATTPE ARTSEDSLLK STLPPSETSA PAEGVRNQTL
110 120 130 140 150
TSTEKAEGVV KLQNLTLPTN ASIKFNPGAE SVVLSNSTLK FLQSFARKSN
160 170 180 190 200
EQATSLNTVG GTGGIGGVGG TGGVGNRAPR ETYLSRGDSS SSQRTDYQKS
210 220 230 240 250
NFETTRGKNW CAYVHTRLSP TVILDNQVTY VPGGKGPCGW TGGSCPQRSQ
260 270 280 290 300
KISNPVYRMQ HKIVTSLDWR CCPGYSGPKC QLRAQEQQSL IHTNQAESHT
310 320 330 340 350
AVGRGVAEQQ QQQGCGDPEV MQKMTDQVNY QAMKLTLLQK KIDNISLTVN
360 370 380 390 400
DVRNTYSSLE GKVSEDKSRE FQSLLKGLKS KSINVLIRDI VREQFKIFQN
410 420 430 440 450
DMQETVAQLF KTVSSLSEDL ESTRQIIQKV NESVVSIAAQ QKFVLVQENR
460 470 480 490 500
PTLTDIVELR NHIVNVRQEM TLTCEKPIKE LEVKQTHLEG ALEQEHSRSI
510 520 530 540 550
LYYESLNKTL SKLKEVHEQL LSTEQVSDQK NAPAAESVSN NVTEYMSTLH
560 570 580 590 600
ENIKKQSLMM LQMFEDLHIQ ESKINNLTVS LEMEKESLRG ECEDMLSKCR
610 620 630 640 650
NDFKFQLKDT EENLHVLNQT LAEVLFPMDN KMDKMSEQLN DLTYDMEILQ
660 670 680 690 700
PLLEQGASLR QTMTYEQPKE AIVIRKKIEN LTSAVNSLNF IIKELTKRHN
710 720 730 740 750
LLRNEVQGRD DALERRINEY ALEMEDGLNK TMTIINNAID FIQDNYALKE
760 770 780 790 800
TLSTIKDNSE IHHKCTSDME TILTFIPQFH RLNDSIQTLV NDNQRYNFVL
810 820 830 840 850
QVAKTLAGIP RDEKLNQSNF QKMYQMFNET TSQVRKYQQN MSHLEEKLLL
860 870 880 890 900
TTKISKNFET RLQDIESKVT QTLIPYYISV KKGSVVTNER DQALQLQVLN
910 920 930 940 950
SRFKALEAKS IHLSINFFSL NKTLHEVLTM CHNASTSVSE LNATIPKWIK
960 970 980 990 1000
HSLPDIQLLQ KGLTEFVEPI IQIKTQAALS NLTCCIDRSL PGSLANVVKS
1010 1020 1030 1040 1050
QKQVKSLPKK INALKKPTVN LTTVLIGRTQ RNTDNIIYPE EYSSCSRHPC
1060 1070 1080 1090 1100
QNGGTCINGR TSFTCACRHP FTGDNCTIKL VEENALAPDF SKGSYRYAPM
1110 1120 1130 1140 1150
VAFFASHTYG MTIPGPILFN NLDVNYGASY TPRTGKFRIP YLGVYVFKYT
1160 1170 1180 1190 1200
IESFSAHISG FLVVDGIDKL AFESENINSE IHCDRVLTGD ALLELNYGQE
1210 1220
VWLRLAKGTI PAKFPPVTTF SGYLLYRT
Length:1,228
Mass (Da):138,110
Last modified:April 3, 2007 - v3
Checksum:i270BCFBE85AA2F8F
GO
Isoform 2 (identifier: Q13201-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     71-104: Missing.
     377-1039: Missing.

Note: No experimental confirmation available.
Show »
Length:531
Mass (Da):58,170
Checksum:i80974ECCBAA1F993
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti217R → K in BAC86201 (PubMed:14702039).Curated1
Sequence conflicti223I → T in AAC52065 (PubMed:7629143).Curated1
Sequence conflicti982L → S in AAC52065 (PubMed:7629143).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03147158T → A. Corresponds to variant dbSNP:rs1442138Ensembl.1
Natural variantiVAR_031472805T → A. Corresponds to variant dbSNP:rs3756065Ensembl.1
Natural variantiVAR_031473883G → D. Corresponds to variant dbSNP:rs12646270Ensembl.1
Natural variantiVAR_031474964T → R1 PublicationCorresponds to variant dbSNP:rs17855885Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_03661071 – 104Missing in isoform 2. 1 PublicationAdd BLAST34
Alternative sequenceiVSP_036611377 – 1039Missing in isoform 2. 1 PublicationAdd BLAST663

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27109 mRNA. Translation: AAC52065.1.
AK125557 mRNA. Translation: BAC86201.1.
AK313566 mRNA. Translation: BAG36340.1.
AC093759 Genomic DNA. Translation: AAY40957.1.
CH471057 Genomic DNA. Translation: EAX06038.1.
BC063848 mRNA. Translation: AAH63848.1.
CCDSiCCDS3635.1. [Q13201-1]
PIRiA57384.
RefSeqiNP_031377.2. NM_007351.2. [Q13201-1]
XP_016863382.1. XM_017007893.1. [Q13201-1]
UniGeneiHs.268107.

Genome annotation databases

EnsembliENST00000264790; ENSP00000264790; ENSG00000138722. [Q13201-1]
ENST00000394980; ENSP00000378431; ENSG00000138722. [Q13201-1]
GeneIDi22915.
KEGGihsa:22915.
UCSCiuc003hst.4. human. [Q13201-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiMMRN1_HUMAN
AccessioniPrimary (citable) accession number: Q13201
Secondary accession number(s): Q4W5L1, Q6P3T8, Q6ZUL9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: April 3, 2007
Last modified: September 27, 2017
This is version 159 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot