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Protein

Serpin B7

Gene

Serpinb7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Might function as an inhibitor of Lys-specific proteases. Might influence the maturation of megakaryocytes via its action as a serpin (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei347 – 3482Reactive bondBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI04.012.

Names & Taxonomyi

Protein namesi
Recommended name:
Serpin B7
Alternative name(s):
Megsin
Gene namesi
Name:Serpinb7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2151053. Serpinb7.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 380380Serpin B7PRO_0000094109Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei217 – 2171PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9D695.
PRIDEiQ9D695.

PTM databases

PhosphoSiteiQ9D695.

Expressioni

Gene expression databases

BgeeiQ9D695.
ExpressionAtlasiQ9D695. baseline and differential.
GenevisibleiQ9D695. MM.

Interactioni

Protein-protein interaction databases

BioGridi228047. 1 interaction.
STRINGi10090.ENSMUSP00000083896.

Structurei

3D structure databases

ProteinModelPortaliQ9D695.
SMRiQ9D695. Positions 3-380.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the serpin family. Ov-serpin subfamily.Curated

Phylogenomic databases

eggNOGiKOG2392. Eukaryota.
COG4826. LUCA.
GeneTreeiENSGT00760000118789.
HOGENOMiHOG000238519.
HOVERGENiHBG005957.
InParanoidiQ9D695.
KOiK13964.
OMAiKSETLHC.
PhylomeDBiQ9D695.
TreeFamiTF352619.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D695-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASLAAANAE FGFDLFREMD SSQGNGNVFF SSLSIFTALT LIRLGARGDC
60 70 80 90 100
ARQIDKALHF NIPSRQGNSS NNQPGLQYQL KRVLADINSS HKDYELSIAT
110 120 130 140 150
GVFAEKVYDF HKNYIECAEN LYNAKVERVD FTNDVQDTRF KINKWIENET
160 170 180 190 200
HGKIKKVLGD SSLSSSAVMV LVNAVYFKGK WKSAFTKTDT LSCRFRSPTC
210 220 230 240 250
PGKVVNMMHQ ERRFNLSTIQ QPPMQVLELQ YHGGISMYIM LPEDGLCEIE
260 270 280 290 300
SKLSFQNLMD WTNRRKMKSQ YVNVFLPQFK IEKNYEMTHH LKSLGLKDIF
310 320 330 340 350
DESSADLSGI ASGGRLYVSK LMHKSFIEVS EEGTEATAAT ENNIVEKQLP
360 370 380
ESTVFRADRP FLFVIKKNDI ILFTGKVSCP
Length:380
Mass (Da):43,050
Last modified:June 1, 2001 - v1
Checksum:iC9240272BCFB9CF4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF105328 mRNA. Translation: AAL16768.1.
AK014524 mRNA. Translation: BAB29410.1.
CCDSiCCDS35686.1.
RefSeqiNP_081824.1. NM_027548.3.
XP_006529149.1. XM_006529086.1.
UniGeneiMm.66015.

Genome annotation databases

EnsembliENSMUST00000086690; ENSMUSP00000083896; ENSMUSG00000067001.
GeneIDi116872.
KEGGimmu:116872.
UCSCiuc007chm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF105328 mRNA. Translation: AAL16768.1.
AK014524 mRNA. Translation: BAB29410.1.
CCDSiCCDS35686.1.
RefSeqiNP_081824.1. NM_027548.3.
XP_006529149.1. XM_006529086.1.
UniGeneiMm.66015.

3D structure databases

ProteinModelPortaliQ9D695.
SMRiQ9D695. Positions 3-380.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi228047. 1 interaction.
STRINGi10090.ENSMUSP00000083896.

Protein family/group databases

MEROPSiI04.012.

PTM databases

PhosphoSiteiQ9D695.

Proteomic databases

PaxDbiQ9D695.
PRIDEiQ9D695.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000086690; ENSMUSP00000083896; ENSMUSG00000067001.
GeneIDi116872.
KEGGimmu:116872.
UCSCiuc007chm.2. mouse.

Organism-specific databases

CTDi8710.
MGIiMGI:2151053. Serpinb7.

Phylogenomic databases

eggNOGiKOG2392. Eukaryota.
COG4826. LUCA.
GeneTreeiENSGT00760000118789.
HOGENOMiHOG000238519.
HOVERGENiHBG005957.
InParanoidiQ9D695.
KOiK13964.
OMAiKSETLHC.
PhylomeDBiQ9D695.
TreeFamiTF352619.

Miscellaneous databases

NextBioi369246.
PROiQ9D695.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D695.
ExpressionAtlasiQ9D695. baseline and differential.
GenevisibleiQ9D695. MM.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of rodent megsin revealed its up-regulation in mesangioproliferative nephritis."
    Nangaku M., Miyata T., Suzuki D., Umezono T., Hashimoto T., Wada T., Yagi M., Nagano N., Inagi R., Kurokawa K.
    Kidney Int. 60:641-652(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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.
    , 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].
    Strain: C57BL/6J.
    Tissue: Skin.

Entry informationi

Entry nameiSPB7_MOUSE
AccessioniPrimary (citable) accession number: Q9D695
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

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 one 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.