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Protein

Mannan-binding lectin serine protease 2

Gene

Masp2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase (By similarity).By similarity

Catalytic activityi

Selective cleavage after Arg-223 in complement component C2 (-Ser-Leu-Gly-Arg-|-Lys-Ile-Gln-Ile) and after Arg-76 in complement component C4 (-Gly-Leu-Gln-Arg-|-Ala-Leu-Glu-Ile).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi67 – 671Calcium 1By similarity
Metal bindingi75 – 751Calcium 1By similarity
Metal bindingi120 – 1201Calcium 1By similarity
Metal bindingi122 – 1221Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi123 – 1231Calcium 1By similarity
Metal bindingi138 – 1381Calcium 2By similarity
Metal bindingi141 – 1411Calcium 2By similarity
Metal bindingi158 – 1581Calcium 2By similarity
Metal bindingi162 – 1621Calcium 2; via carbonyl oxygenBy similarity
Sitei443 – 4442CleavageBy similarity
Active sitei483 – 4831Charge relay systemBy similarity
Active sitei532 – 5321Charge relay systemBy similarity
Active sitei632 – 6321Charge relay systemBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Complement pathway, Immunity, Innate immunity

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.21.104. 3474.

Protein family/group databases

MEROPSiS01.229.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannan-binding lectin serine protease 2 (EC:3.4.21.104)
Alternative name(s):
MBL-associated serine protease 2
Mannose-binding protein-associated serine protease 2
Short name:
MASP-2
Cleaved into the following 2 chains:
Gene namesi
Name:Masp2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1330832. Masp2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919By similarityAdd
BLAST
Chaini20 – 685666Mannan-binding lectin serine protease 2PRO_0000027601Add
BLAST
Chaini20 – 443424Mannan-binding lectin serine protease 2 A chainPRO_0000027602Add
BLAST
Chaini444 – 685242Mannan-binding lectin serine protease 2 B chainPRO_0000027603Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi72 ↔ 90By similarity
Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi142 ↔ 156By similarity
Disulfide bondi152 ↔ 165By similarity
Modified residuei158 – 1581(3R)-3-hydroxyasparagineSequence Analysis
Disulfide bondi167 ↔ 180By similarity
Disulfide bondi184 ↔ 211By similarity
Disulfide bondi241 ↔ 259By similarity
Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi300 ↔ 348By similarity
Glycosylationi308 – 3081N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi328 ↔ 361By similarity
Disulfide bondi366 ↔ 411By similarity
Disulfide bondi396 ↔ 429By similarity
Disulfide bondi433 ↔ 552Interchain (between A and B chains)PROSITE-ProRule annotation
Glycosylationi545 – 5451N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi598 ↔ 617By similarity
Disulfide bondi628 ↔ 659By similarity
Glycosylationi641 – 6411N-linked (GlcNAc...)1 Publication

Post-translational modificationi

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.By similarity

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

MaxQBiQ91WP0.
PaxDbiQ91WP0.
PRIDEiQ91WP0.

PTM databases

PhosphoSiteiQ91WP0.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiQ91WP0.
CleanExiMM_MASP2.
GenevestigatoriQ91WP0.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Binds MBL2. Isoform 2 binds to MASP1. Binds SERPING1 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000101327.

Structurei

3D structure databases

ProteinModelPortaliQ91WP0.
SMRiQ91WP0. Positions 24-685.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 137118CUB 1PROSITE-ProRule annotationAdd
BLAST
Domaini138 – 18144EGF-like; calcium-bindingAdd
BLAST
Domaini184 – 296113CUB 2PROSITE-ProRule annotationAdd
BLAST
Domaini298 – 36366Sushi 1PROSITE-ProRule annotationAdd
BLAST
Domaini364 – 43168Sushi 2PROSITE-ProRule annotationAdd
BLAST
Domaini444 – 683240Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 2 CUB domains.PROSITE-ProRule annotation
Contains 1 EGF-like domain.Curated
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
Contains 2 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Sushi

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118890.
HOVERGENiHBG000559.
InParanoidiQ91WP0.
KOiK03993.
OMAiWTLTAPP.
OrthoDBiEOG7W6WK4.
PhylomeDBiQ91WP0.
TreeFamiTF330373.

Family and domain databases

Gene3Di2.60.120.290. 2 hits.
InterProiIPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024175. Pept_S1A_C1r/C1S/mannan-bd.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00431. CUB. 2 hits.
PF07645. EGF_CA. 1 hit.
PF00084. Sushi. 2 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001155. C1r_C1s_MASP. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00032. CCP. 2 hits.
SM00042. CUB. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 2 hits.
SSF50494. SSF50494. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS01180. CUB. 2 hits.
PS01186. EGF_2. 1 hit.
PS01187. EGF_CA. 1 hit.
PS50923. SUSHI. 2 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

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: Q91WP0-1) [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
MRLLIFLGLL WSLVATLLGS KWPEPVFGRL VSPGFPEKYA DHQDRSWTLT
60 70 80 90 100
APPGYRLRLY FTHFDLELSY RCEYDFVKLS SGTKVLATLC GQESTDTEQA
110 120 130 140 150
PGNDTFYSLG PSLKVTFHSD YSNEKPFTGF EAFYAAEDVD ECRVSLGDSV
160 170 180 190 200
PCDHYCHNYL GGYYCSCRAG YVLHQNKHTC SALCSGQVFT GRSGYLSSPE
210 220 230 240 250
YPQPYPKLSS CTYSIRLEDG FSVILDFVES FDVETHPEAQ CPYDSLKIQT
260 270 280 290 300
DKGEHGPFCG KTLPPRIETD SHKVTITFAT DESGNHTGWK IHYTSTARPC
310 320 330 340 350
PDPTAPPNGS ISPVQAIYVL KDRFSVFCKT GFELLQGSVP LKSFTAVCQK
360 370 380 390 400
DGSWDRPMPE CSIIDCGPPD DLPNGHVDYI TGPEVTTYKA VIQYSCEETF
410 420 430 440 450
YTMSSNGKYV CEADGFWTSS KGEKLPPVCE PVCGLSTHTI GGRIVGGQPA
460 470 480 490 500
KPGDFPWQVL LLGQTTAAAG ALIHDNWVLT AAHAVYEKRM AASSLNIRMG
510 520 530 540 550
ILKRLSPHYT QAWPEEIFIH EGYTHGAGFD NDIALIKLKN KVTINGSIMP
560 570 580 590 600
VCLPRKEAAS LMRTDFTGTV AGWGLTQKGL LARNLMFVDI PIADHQKCTA
610 620 630 640 650
VYEKLYPGVR VSANMLCAGL ETGGKDSCRG DSGGALVFLD NETQRWFVGG
660 670 680
IVSWGSINCG AADQYGVYTK VINYIPWIEN IISNF
Length:685
Mass (Da):75,517
Last modified:December 1, 2001 - v1
Checksum:iF56A6D522BC7099D
GO
Isoform 2 (identifier: Q91WP0-2) [UniParc]FASTAAdd to basket

Also known as: MAp19

The sequence of this isoform differs from the canonical sequence as follows:
     182-185: ALCS → EQSL
     186-685: Missing.

Show »
Length:185
Mass (Da):20,974
Checksum:i72E01900D30A18B9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 22MR → MSLPCPQ (PubMed:10586086).Curated
Sequence conflicti172 – 1721V → I in BAA34674 (PubMed:9794427).Curated
Sequence conflicti172 – 1721V → I in CAB65247 (PubMed:10586086).Curated
Sequence conflicti192 – 1921R → K in CAB65250 (PubMed:10586086).Curated
Sequence conflicti317 – 3171I → T in BAA34674 (PubMed:9794427).Curated
Sequence conflicti325 – 3251S → Y in CAB65250 (PubMed:10586086).Curated
Sequence conflicti384 – 3841E → Q in BAA34674 (PubMed:9794427).Curated
Sequence conflicti600 – 6001A → T in BAA34674 (PubMed:9794427).Curated
Sequence conflicti663 – 6631D → G in BAA34674 (PubMed:9794427).Curated
Sequence conflicti678 – 6781I → N in BAA34674 (PubMed:9794427).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei182 – 1854ALCS → EQSL in isoform 2. 1 PublicationVSP_014636
Alternative sequencei186 – 685500Missing in isoform 2. 1 PublicationVSP_014637Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009459 mRNA. Translation: BAA34674.1.
AJ250369 mRNA. Translation: CAB63701.1.
Y19160 mRNA. Translation: CAB65247.1.
Y19163 mRNA. Translation: CAB65250.1.
AK050052 mRNA. Translation: BAC34052.1.
AL606969 Genomic DNA. Translation: CAM21185.1.
AL606969 Genomic DNA. Translation: CAM21186.1.
BC013893 mRNA. Translation: AAH13893.1.
CCDSiCCDS18941.1. [Q91WP0-1]
CCDS18942.1. [Q91WP0-2]
RefSeqiNP_001003893.1. NM_001003893.2. [Q91WP0-1]
NP_034897.1. NM_010767.3. [Q91WP0-2]
UniGeneiMm.378962.

Genome annotation databases

EnsembliENSMUST00000052060; ENSMUSP00000049729; ENSMUSG00000028979. [Q91WP0-1]
ENSMUST00000105701; ENSMUSP00000101326; ENSMUSG00000028979. [Q91WP0-2]
GeneIDi17175.
KEGGimmu:17175.
UCSCiuc008vux.1. mouse. [Q91WP0-2]
uc008vuy.1. mouse. [Q91WP0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009459 mRNA. Translation: BAA34674.1.
AJ250369 mRNA. Translation: CAB63701.1.
Y19160 mRNA. Translation: CAB65247.1.
Y19163 mRNA. Translation: CAB65250.1.
AK050052 mRNA. Translation: BAC34052.1.
AL606969 Genomic DNA. Translation: CAM21185.1.
AL606969 Genomic DNA. Translation: CAM21186.1.
BC013893 mRNA. Translation: AAH13893.1.
CCDSiCCDS18941.1. [Q91WP0-1]
CCDS18942.1. [Q91WP0-2]
RefSeqiNP_001003893.1. NM_001003893.2. [Q91WP0-1]
NP_034897.1. NM_010767.3. [Q91WP0-2]
UniGeneiMm.378962.

3D structure databases

ProteinModelPortaliQ91WP0.
SMRiQ91WP0. Positions 24-685.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000101327.

Protein family/group databases

MEROPSiS01.229.

PTM databases

PhosphoSiteiQ91WP0.

Proteomic databases

MaxQBiQ91WP0.
PaxDbiQ91WP0.
PRIDEiQ91WP0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000052060; ENSMUSP00000049729; ENSMUSG00000028979. [Q91WP0-1]
ENSMUST00000105701; ENSMUSP00000101326; ENSMUSG00000028979. [Q91WP0-2]
GeneIDi17175.
KEGGimmu:17175.
UCSCiuc008vux.1. mouse. [Q91WP0-2]
uc008vuy.1. mouse. [Q91WP0-1]

Organism-specific databases

CTDi10747.
MGIiMGI:1330832. Masp2.

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118890.
HOVERGENiHBG000559.
InParanoidiQ91WP0.
KOiK03993.
OMAiWTLTAPP.
OrthoDBiEOG7W6WK4.
PhylomeDBiQ91WP0.
TreeFamiTF330373.

Enzyme and pathway databases

BRENDAi3.4.21.104. 3474.

Miscellaneous databases

ChiTaRSiMasp2. mouse.
NextBioi291480.
PROiQ91WP0.
SOURCEiSearch...

Gene expression databases

BgeeiQ91WP0.
CleanExiMM_MASP2.
GenevestigatoriQ91WP0.

Family and domain databases

Gene3Di2.60.120.290. 2 hits.
InterProiIPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024175. Pept_S1A_C1r/C1S/mannan-bd.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00431. CUB. 2 hits.
PF07645. EGF_CA. 1 hit.
PF00084. Sushi. 2 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001155. C1r_C1s_MASP. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00032. CCP. 2 hits.
SM00042. CUB. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 2 hits.
SSF50494. SSF50494. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS01180. CUB. 2 hits.
PS01186. EGF_2. 1 hit.
PS01187. EGF_CA. 1 hit.
PS50923. SUSHI. 2 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two lineages of mannose-binding lectin-associated serine protease (MASP) in vertebrates."
    Endo Y., Takahashi M., Nakao M., Saiga H., Sekine H., Matsushita M., Nonaka M., Fujita T.
    J. Immunol. 161:4924-4930(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: BALB/c.
    Tissue: Liver.
  2. "The rat and mouse homologues of MASP-2 and MAp19, components of the mannan-binding lectin activation pathway of complement."
    Stover C.M., Thiel S., Lynch N.J., Schwaeble W.J.
    J. Immunol. 163:6848-6859(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 1-362 (ISOFORM 1).
    Strain: C57BL/6J X CBA/J.
  3. "Organization of the MASP2 locus and its expression profile in mouse and rat."
    Stover C.M., Lynch N.J., Hanson S.J., Windbichler M., Gregory S.G., Schwaeble W.J.
    Mamm. Genome 15:887-900(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "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.
    , 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 1).
    Strain: C57BL/6J.
    Tissue: Liver.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "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).
    Strain: FVB/N.
    Tissue: Liver.
  7. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
    Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
    J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-641.
    Strain: C57BL/6.
    Tissue: Plasma.

Entry informationi

Entry nameiMASP2_MOUSE
AccessioniPrimary (citable) accession number: Q91WP0
Secondary accession number(s): B1ARY2
, B1ARY3, Q9QXA4, Q9QXD2, Q9QXD5, Q9Z338
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: December 1, 2001
Last modified: May 27, 2015
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Dimerization and MBL2 binding requires calcium ions.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.