Q13201 (MMRN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

1. Platelet glycoprotein Ia*
2. 155 kDa platelet multimerin
   Short name=p-155
   Short name=p155

Gene names

Name:	MMRN1
Synonyms:	ECM, EMILIN4, GPIA*, MMRN

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1228 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.11 Ref.13
Subunit structure	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. Ref.1 Ref.9 Ref.13
Subcellular location	Secreted Potential.
Tissue specificity	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. Ref.1 Ref.8
Post-translational modification	The N-terminus is blocked. Extensively N-glycosylated.
Involvement in disease	Deficiency in multimerin-1 due to proteolytic degradation within the platelet alpha granules is associated with an autosomal dominant bleeding disorder (factor V Quebec). Ref.14
Sequence similarities	Contains 1 C1q domain. Contains 1 EGF-like domain. Contains 1 EMI domain.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil EGF-like domain Signal
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Traceable author statement PubMed 9189649. Source: ProtInc platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome
Cellular_component	extracellular region Traceable author statement. Source: Reactome platelet alpha granule lumen Traceable author statement. Source: Reactome
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13201-1)

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: Q13201-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 1228	1209	Multimerin-1		PRO_0000007821
	Chain	184 – 1228	1045	Platelet glycoprotein Ia*		PRO_0000367047
	Chain	318 – 1228	911	155 kDa platelet multimerin		PRO_0000367048
Regions
	Domain	207 – 282	76	EMI
	Domain	1041 – 1077	37	EGF-like
	Domain	1096 – 1228	133	C1q
	Coiled coil	333 – 365	33	Potential
	Coiled coil	400 – 430	31	Potential
	Coiled coil	503 – 523	21	Potential
	Coiled coil	580 – 650	71	Potential
	Coiled coil	675 – 726	52	Potential
	Coiled coil	819 – 869	51	Potential
	Motif	186 – 188	3	Cell attachment site Potential
	Compositional bias	189 – 192	4	Poly-Ser
	Compositional bias	309 – 313	5	Poly-Gln
Amino acid modifications
	Glycosylation	21	1	N-linked (GlcNAc...) Potential
	Glycosylation	97	1	N-linked (GlcNAc...) Potential
	Glycosylation	114	1	N-linked (GlcNAc...) Ref.10 Ref.12
	Glycosylation	120	1	N-linked (GlcNAc...) Ref.10
	Glycosylation	136	1	N-linked (GlcNAc...) Ref.10
	Glycosylation	344	1	N-linked (GlcNAc...) Ref.15
	Glycosylation	431	1	N-linked (GlcNAc...) Potential
	Glycosylation	507	1	N-linked (GlcNAc...) Potential
	Glycosylation	541	1	N-linked (GlcNAc...) Potential
	Glycosylation	576	1	N-linked (GlcNAc...) Potential
	Glycosylation	618	1	N-linked (GlcNAc...) Ref.10
	Glycosylation	680	1	N-linked (GlcNAc...) Potential
	Glycosylation	729	1	N-linked (GlcNAc...) Ref.10 Ref.15
	Glycosylation	783	1	N-linked (GlcNAc...) Potential
	Glycosylation	816	1	N-linked (GlcNAc...) Potential
	Glycosylation	828	1	N-linked (GlcNAc...) Potential
	Glycosylation	840	1	N-linked (GlcNAc...) Potential
	Glycosylation	921	1	N-linked (GlcNAc...) Potential
	Glycosylation	933	1	N-linked (GlcNAc...) Potential
	Glycosylation	942	1	N-linked (GlcNAc...) Ref.15
	Glycosylation	981	1	N-linked (GlcNAc...) Potential
	Glycosylation	1020	1	N-linked (GlcNAc...) Ref.15
	Glycosylation	1075	1	N-linked (GlcNAc...) Potential
	Disulfide bond	211 ↔ 272		By similarity
	Disulfide bond	238 ↔ 245		By similarity
	Disulfide bond	271 ↔ 280		By similarity
	Disulfide bond	1045 ↔ 1056		By similarity
	Disulfide bond	1050 ↔ 1065		By similarity
	Disulfide bond	1067 ↔ 1076		By similarity
Natural variations
	Alternative sequence	71 – 104	34	Missing in isoform 2.		VSP_036610
	Alternative sequence	377 – 1039	663	Missing in isoform 2.		VSP_036611
	Natural variant	58	1	T → A. Corresponds to variant rs1442138 [ dbSNP | Ensembl ].		VAR_031471
	Natural variant	805	1	T → A. Corresponds to variant rs3756065 [ dbSNP | Ensembl ].		VAR_031472
	Natural variant	883	1	G → D. Corresponds to variant rs12646270 [ dbSNP | Ensembl ].		VAR_031473
	Natural variant	964	1	T → R. Ref.5 Corresponds to variant rs17855885 [ dbSNP | Ensembl ].		VAR_031474
Experimental info
	Sequence conflict	217	1	R → K in BAC86201. Ref.2
	Sequence conflict	223	1	I → T in AAC52065. Ref.1
	Sequence conflict	982	1	L → S in AAC52065. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 3, 2007. Version 3. Checksum: 270BCFBE85AA2F8F	FASTA	1,228	138,110
	10 20 30 40 50 60 MKGARLFVLL SSLWSGGIGL NNSKHSWTIP EDGNSQKTMP SASVPPNKIQ SLQILPTTRV 70 80 90 100 110 120 MSAEIATTPE ARTSEDSLLK STLPPSETSA PAEGVRNQTL TSTEKAEGVV KLQNLTLPTN 130 140 150 160 170 180 ASIKFNPGAE SVVLSNSTLK FLQSFARKSN EQATSLNTVG GTGGIGGVGG TGGVGNRAPR 190 200 210 220 230 240 ETYLSRGDSS SSQRTDYQKS NFETTRGKNW CAYVHTRLSP TVILDNQVTY VPGGKGPCGW 250 260 270 280 290 300 TGGSCPQRSQ KISNPVYRMQ HKIVTSLDWR CCPGYSGPKC QLRAQEQQSL IHTNQAESHT 310 320 330 340 350 360 AVGRGVAEQQ QQQGCGDPEV MQKMTDQVNY QAMKLTLLQK KIDNISLTVN DVRNTYSSLE 370 380 390 400 410 420 GKVSEDKSRE FQSLLKGLKS KSINVLIRDI VREQFKIFQN DMQETVAQLF KTVSSLSEDL 430 440 450 460 470 480 ESTRQIIQKV NESVVSIAAQ QKFVLVQENR PTLTDIVELR NHIVNVRQEM TLTCEKPIKE 490 500 510 520 530 540 LEVKQTHLEG ALEQEHSRSI LYYESLNKTL SKLKEVHEQL LSTEQVSDQK NAPAAESVSN 550 560 570 580 590 600 NVTEYMSTLH ENIKKQSLMM LQMFEDLHIQ ESKINNLTVS LEMEKESLRG ECEDMLSKCR 610 620 630 640 650 660 NDFKFQLKDT EENLHVLNQT LAEVLFPMDN KMDKMSEQLN DLTYDMEILQ PLLEQGASLR 670 680 690 700 710 720 QTMTYEQPKE AIVIRKKIEN LTSAVNSLNF IIKELTKRHN LLRNEVQGRD DALERRINEY 730 740 750 760 770 780 ALEMEDGLNK TMTIINNAID FIQDNYALKE TLSTIKDNSE IHHKCTSDME TILTFIPQFH 790 800 810 820 830 840 RLNDSIQTLV NDNQRYNFVL QVAKTLAGIP RDEKLNQSNF QKMYQMFNET TSQVRKYQQN 850 860 870 880 890 900 MSHLEEKLLL TTKISKNFET RLQDIESKVT QTLIPYYISV KKGSVVTNER DQALQLQVLN 910 920 930 940 950 960 SRFKALEAKS IHLSINFFSL NKTLHEVLTM CHNASTSVSE LNATIPKWIK HSLPDIQLLQ 970 980 990 1000 1010 1020 KGLTEFVEPI IQIKTQAALS NLTCCIDRSL PGSLANVVKS QKQVKSLPKK INALKKPTVN 1030 1040 1050 1060 1070 1080 LTTVLIGRTQ RNTDNIIYPE EYSSCSRHPC QNGGTCINGR TSFTCACRHP FTGDNCTIKL 1090 1100 1110 1120 1130 1140 VEENALAPDF SKGSYRYAPM VAFFASHTYG MTIPGPILFN NLDVNYGASY TPRTGKFRIP 1150 1160 1170 1180 1190 1200 YLGVYVFKYT IESFSAHISG FLVVDGIDKL AFESENINSE IHCDRVLTGD ALLELNYGQE 1210 1220 VWLRLAKGTI PAKFPPVTTF SGYLLYRT
	Isoform 2 [UniParc]. Checksum: 80974ECCBAA1F993	FASTA	531	58,170
	10 20 30 40 50 60 MKGARLFVLL SSLWSGGIGL NNSKHSWTIP EDGNSQKTMP SASVPPNKIQ SLQILPTTRV 70 80 90 100 110 120 MSAEIATTPE KAEGVVKLQN LTLPTNASIK FNPGAESVVL SNSTLKFLQS FARKSNEQAT 130 140 150 160 170 180 SLNTVGGTGG IGGVGGTGGV GNRAPRETYL SRGDSSSSQR TDYQKSNFET TRGKNWCAYV 190 200 210 220 230 240 HTRLSPTVIL DNQVTYVPGG KGPCGWTGGS CPQRSQKISN PVYRMQHKIV TSLDWRCCPG 250 260 270 280 290 300 YSGPKCQLRA QEQQSLIHTN QAESHTAVGR GVAEQQQQQG CGDPEVMQKM TDQVNYQAMK 310 320 330 340 350 360 LTLLQKKIDN ISLTVNDVRN TYSSLEGKVS EDKSREFQSL LKEEYSSCSR HPCQNGGTCI 370 380 390 400 410 420 NGRTSFTCAC RHPFTGDNCT IKLVEENALA PDFSKGSYRY APMVAFFASH TYGMTIPGPI 430 440 450 460 470 480 LFNNLDVNYG ASYTPRTGKF RIPYLGVYVF KYTIESFSAH ISGFLVVDGI DKLAFESENI 490 500 510 520 530 NSEIHCDRVL TGDALLELNY GQEVWLRLAK GTIPAKFPPV TTFSGYLLYR T

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The cDNA sequence of human endothelial cell multimerin. A unique protein with RGDS, coiled-coil, and epidermal growth factor-like domains and a carboxyl terminus similar to the globular domain of complement C1q and collagens type VIII and X." Hayward C.P.M., Hassell J.A., Denomme G.A., Rachubinski R.A., Brown C., Kelton J.G. J. Biol. Chem. 270:18246-18251(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 368-376, FUNCTION, SUBUNIT, TISSUE SPECIFICITY. Tissue: Endothelial cell.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
[3]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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 1), VARIANT ARG-964. Tissue: PNS.
[6]	"Platelet glycoprotein Ia* is the processed form of multimerin --isolation and determination of N-terminal sequences of stored and released forms." Polgar J., Magnenat E., Wells T.N.C., Clemetson K.J. Thromb. Haemost. 80:645-648(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 184-198 AND 318-326.
[7]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 461-467. Tissue: Platelet.
[8]	"Multimerin is found in the alpha-granules of resting platelets and is synthesized by a megakaryocytic cell line." Hayward C.P.M., Bainton D.F., Smith J.W., Horsewood P., Stead R.H., Podor T.J., Warkentin T.E., Kelton J.G. J. Clin. Invest. 91:2630-2639(1993) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[9]	"Platelet multimerin and its proteolytic processing." Hayward C.P.M. Thromb. Haemost. 82:1779-1780(1999) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT.
[10]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-114; ASN-120; ASN-136; ASN-618 AND ASN-729, MASS SPECTROMETRY. Tissue: Plasma.
[11]	"Analyses of cellular multimerin 1 receptors: in vitro evidence of binding mediated by alphaIIbbeta3 and alphavbeta3." Adam F., Zheng S., Joshi N., Kelton D.S., Sandhu A., Suehiro Y., Jeimy S.B., Santos A.V., Masse J.-M., Kelton J.G., Cramer E.M., Hayward C.P.M. Thromb. Haemost. 94:1004-1011(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach." Lewandrowski U., Moebius J., Walter U., Sickmann A. Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-114, MASS SPECTROMETRY. Tissue: Platelet.
[13]	"Multimerin 1 binds factor V and activated factor V with high affinity and inhibits thrombin generation." Jeimy S.B., Fuller N., Tasneem S., Segers K., Stafford A.R., Weitz J.I., Camire R.M., Nicolaes G.A.F., Hayward C.P.M. Thromb. Haemost. 100:1058-1067(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH FACTOR V.
[14]	"An autosomal dominant, qualitative platelet disorder associated with multimerin deficiency, abnormalities in platelet factor V, thrombospondin, von Willebrand factor, and fibrinogen and an epinephrine aggregation defect." Hayward C.P.M., Rivard G.E., Kane W.H., Drouin J., Zheng S., Moore J.C., Kelton J.G. Blood 87:4967-4978(1996) [PubMed] [Europe PMC] [Abstract] Cited for: DISEASE.
[15]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-344; ASN-729; ASN-942 AND ASN-1020, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00012269. IPI00745154.
PIR	A57384.
RefSeq	NP_031377.2. NM_007351.2.
UniGene	Hs.268107.
3D structure databases
ProteinModelPortal	Q13201.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13201. 1 interaction.
STRING	9606.ENSP00000264790.
PTM databases
PhosphoSite	Q13201.
Polymorphism databases
DMDM	143811421.
2D gel databases
OGP	Q13201.
Proteomic databases
PaxDb	Q13201.
PRIDE	Q13201.
Protocols and materials databases
DNASU	22915.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264790; ENSP00000264790; ENSG00000138722. ENST00000394980; ENSP00000378431; ENSG00000138722. ENST00000394981; ENSP00000378432; ENSG00000138722.
GeneID	22915.
KEGG	hsa:22915.
UCSC	uc003hst.3. human. uc010iku.3. human.
Organism-specific databases
CTD	22915.
GeneCards	GC04P090800.
H-InvDB	HIX0024584.
HGNC	HGNC:7178. MMRN1.
HPA	HPA035769.
MIM	601456. gene.
neXtProt	NX_Q13201.
PharmGKB	PA30891.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG45481.
HOGENOM	HOG000113610.
HOVERGEN	HBG108139.
InParanoid	Q13201.
OMA	KFRIPYL.
OrthoDB	EOG4X3H0J.
PhylomeDB	Q13201.
Enzyme and pathway databases
Reactome	REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	Q13201.
Bgee	Q13201.
CleanEx	HS_MMRN1.
Genevestigator	Q13201.
GermOnline	ENSG00000138722. Homo sapiens.
Family and domain databases
Gene3D	2.60.120.40. 1 hit.
InterPro	IPR001073. C1q. IPR000742. EG-like_dom. IPR013032. EGF-like_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR011489. EMI_domain. IPR008983. Tumour_necrosis_fac-like_dom. [Graphical view]
Pfam	PF00386. C1q. 1 hit. PF00008. EGF. 1 hit. PF07546. EMI. 1 hit. [Graphical view]
PRINTS	PR00007. COMPLEMNTC1Q.
SMART	SM00110. C1Q. 1 hit. SM00181. EGF. 1 hit. [Graphical view]
SUPFAM	SSF49842. TNF_like. 1 hit.
PROSITE	PS50871. C1Q. 1 hit. PS00022. EGF_1. 1 hit. PS01186. EGF_2. 1 hit. PS50026. EGF_3. 1 hit. PS51041. EMI. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	22915.
NextBio	43599.
SOURCE	Search...

Entry information

Entry name

MMRN1_HUMAN

Accession

Primary (citable) accession number: Q13201
Secondary accession number(s): Q4W5L1, Q6P3T8, Q6ZUL9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	April 3, 2007
Last modified:	May 1, 2013
This is version 125 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.