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Q63041

- A1M_RAT

UniProt

Q63041 - A1M_RAT

Protein

Alpha-1-macroglobulin

Gene

A1m

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase By similarity.By similarity

    GO - Molecular functioni

    1. protein complex binding Source: RGD
    2. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

    GO - Biological processi

    1. embryo implantation Source: Ensembl

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-1-macroglobulin
    Short name:
    Alpha-1-M
    Alternative name(s):
    Alpha-1-macroglobulin 165 kDa subunit
    Cleaved into the following chain:
    Gene namesi
    Name:A1mImported
    Synonyms:PzpImported
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 4

    Organism-specific databases

    RGDi628643. Pzp.

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular space Source: InterPro

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24241 PublicationAdd
    BLAST
    Chaini25 – 15001476Alpha-1-macroglobulinPRO_0000271403Add
    BLAST
    Chaini1245 – 1500256Alpha-1-macroglobulin 45 kDa subunit1 PublicationPRO_0000271404Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi48 ↔ 86By similarity
    Glycosylationi55 – 551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi61 – 611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi157 – 1571N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi249 ↔ 298By similarity
    Disulfide bondi267 ↔ 286By similarity
    Disulfide bondi277 – 277Interchain (with C-430)By similarity
    Glycosylationi382 – 3821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi412 – 4121N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi430 – 430Interchain (with C-277)By similarity
    Disulfide bondi469 ↔ 562By similarity
    Glycosylationi568 – 5681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi594 ↔ 785By similarity
    Disulfide bondi642 ↔ 689By similarity
    Disulfide bondi835 ↔ 863By similarity
    Disulfide bondi861 ↔ 897By similarity
    Glycosylationi883 – 8831N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi935 ↔ 1344By similarity
    Glycosylationi944 – 9441N-linked (GlcNAc...)Sequence Analysis
    Cross-linki986 ↔ 989Isoglutamyl cysteine thioester (Cys-Gln)By similarity
    Glycosylationi1005 – 10051N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1094 ↔ 1142By similarity
    Glycosylationi1390 – 13901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1448 – 14481N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Thioester bond

    Proteomic databases

    PaxDbiQ63041.
    PRIDEiQ63041.

    Expressioni

    Tissue specificityi

    Widely expressed. Highest level in ovary, testis, uterus and prostate. Protein found in plasma.1 Publication

    Gene expression databases

    GenevestigatoriQ63041.

    Interactioni

    Subunit structurei

    Homotetramer; disulfide-linked.By similarity

    Protein-protein interaction databases

    IntActiQ63041. 1 interaction.
    STRINGi10116.ENSRNOP00000009467.

    Structurei

    Secondary structure

    1
    1500
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1364 – 137512
    Turni1376 – 13783
    Beta strandi1384 – 139310
    Beta strandi1395 – 13995
    Beta strandi1401 – 14088
    Beta strandi1413 – 14153
    Helixi1417 – 14215
    Helixi1422 – 14254
    Beta strandi1429 – 14357
    Beta strandi1438 – 14447
    Beta strandi1451 – 146111
    Beta strandi1469 – 14779
    Beta strandi1481 – 14877

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EDYX-ray2.30A/B1362-1495[»]
    ProteinModelPortaliQ63041.
    SMRiQ63041. Positions 124-225, 1362-1495.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ63041.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni686 – 74661Bait regionBy similarityAdd
    BLAST
    Regioni1360 – 1500141Receptor-binding domain1 PublicationAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Bait region, Signal

    Phylogenomic databases

    eggNOGiCOG2373.
    GeneTreeiENSGT00740000115177.
    HOGENOMiHOG000220939.
    HOVERGENiHBG000039.
    InParanoidiQ63041.
    OMAiTHITNAF.
    OrthoDBiEOG7DJSKB.
    PhylomeDBiQ63041.
    TreeFamiTF313285.

    Family and domain databases

    Gene3Di1.50.10.20. 1 hit.
    2.60.40.690. 1 hit.
    InterProiIPR009048. A-macroglobulin_rcpt-bd.
    IPR011626. A2M_comp.
    IPR002890. A2M_N.
    IPR011625. A2M_N_2.
    IPR014756. Ig_E-set.
    IPR001599. Macroglobln_a2.
    IPR019742. MacrogloblnA2_CS.
    IPR019565. MacrogloblnA2_thiol-ester-bond.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    [Graphical view]
    PfamiPF00207. A2M. 1 hit.
    PF07678. A2M_comp. 1 hit.
    PF01835. A2M_N. 1 hit.
    PF07703. A2M_N_2. 1 hit.
    PF07677. A2M_recep. 1 hit.
    PF10569. Thiol-ester_cl. 1 hit.
    [Graphical view]
    SUPFAMiSSF48239. SSF48239. 1 hit.
    SSF49410. SSF49410. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEiPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q63041-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRRNQLPIPV FLLLLLLLPR DATAATGKPR YVVLVPSELY AGVPEKVCVH     50
    LNHLNETVTL NVTLEYGVQY SNLLIDQAVD KDSSYCSSFT ISRPLSPSAL 100
    IAVEIKGPTH HFIKKKSMWI TKAESPVFVQ TDKPIYKPGQ TVKFRVVSVD 150
    ISFRPVNETF PVVYIENPKR NRIFQWQNVD LPGGLHQLSF PLSVEPALGI 200
    YKVVVQKDSG KKIEHSFEVK EYVLPKFEVQ VKMPKTMAFL EEELVVTACG 250
    LYTYGKPVPG LVTMKVCRKY TQSYSNCHGQ HSKSICEEFS KQADEKGCFR 300
    QVVKTKVFQP RQKGYDMKIE VEAKIKEDGT GIELTGTGSC EIANTLSKLK 350
    FTKANTFYRP GLPFFGQVLL VDEKGQPIPN KNLTVQVNSV RSQFTFTTDE 400
    HGLANILIDT TNFTFSFMGI RVIYKQNNIC FDNWWVDEYH TQADHSAARI 450
    FSPSRSYIQL ELVLGTLACG QTQEIRIHFL LNEDALKDAK DLTFYYLIKA 500
    RGSIFNSGSH VLPLEQGKVK GVVSFPIRVE PGMAPVAKLI VYTILPNEEL 550
    IADVQKFDIE KCFANTVNLS FPSAQSLPAS DTHLTVKATP LSLCALTAVD 600
    QSVLLLKPEA KLSPQSIYNL LPQKAEQGAY LGPLPYKGGE NCIKAEDITH 650
    NGIVYTPKQD LNDNDAYSVF QSIGLKIFTN TRVHKPRYCP MYQAYPPLPY 700
    VGEPQALAMS AIPGAGYRSS NIRTSSMMMM GASEVAQEVE VRETVRKYFP 750
    ETWIWDMVPL DLSGDGELPV KVPDTITEWK ASAFCLSGTT GLGLSSTISH 800
    KVFQPFFLEL TLPYSVVRGE AFILKATVLN YMPHCIRIHV SLEMSPDFLA 850
    VPVGSHEDSH CICGNERKTV SWAVTPKSLG EVNFTATAEA LQSPELCGNK 900
    VAEVPALVQK DTVVKPVIVE PEGIEKEQTY NTLLCPQDAE LQENWTLDLP 950
    ANVVEGSARA TQSVLGDILG SAMQNLQNLL QMPYGCGEQN MVLFVPNIYV 1000
    LEYLNETQQL TEAIKSKAIS YLISGYQRQL NYQHSDGSYS TFGDRGMRHS 1050
    QGNTWLTAFV LKAFAQAQSY IYIEKTHITN AFNWLSMKQR ENGCFQQSGS 1100
    LLNNAMKGGV DDEVTLSAYI TIALLEMPLP VTHSVVRNAL FCLETAWASI 1150
    SNSQESHVYT KALLAYAFAL AGNRAKRSEV LESLNKDAVN EEESVHWQRP 1200
    KNVEENVREM RSFSYKPRAP SAEVEMTAYV LLAYLTSASS RPTRDLSSSD 1250
    LTTASKIVKW ISKQQNSHGG FSSTQDTVVA LQALSKYGAA TFTKSNKEVS 1300
    VTIESSGTVS GTLHVNNGNR LLLQEVRLAD LPGNYITKVS GSGCVYLQTS 1350
    LKYNILPEAE GEAPFTLKVN TLPLNFDKAE HHRKFQIHIN VSYIGERPNS 1400
    NMVIVDVKMV SGFIPVKPSV KKLQDQSNIQ RTEVNTNHVL IYIEKLTNQT 1450
    MGFSFAVEQD IPVKNLKPAP VKVYDYYETD EFAIEEYSAP FSSDSEQGNA 1500
    Length:1,500
    Mass (Da):167,125
    Last modified:November 1, 1996 - v1
    Checksum:i8ABB810985795AB2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti50 – 501H → A AA sequence (PubMed:1725450)Curated
    Sequence conflicti918 – 9181I → P AA sequence (PubMed:1725450)Curated
    Sequence conflicti924 – 9252IE → AT AA sequence (PubMed:1725450)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77183 mRNA. Translation: AAA40723.1.
    M84000 mRNA. Translation: AAA41591.1.
    PIRiA42210.
    RefSeqiNP_665722.2. NM_145779.2.
    UniGeneiRn.11295.

    Genome annotation databases

    EnsembliENSRNOT00000009467; ENSRNOP00000009467; ENSRNOG00000006709.
    GeneIDi252922.
    KEGGirno:252922.
    UCSCiRGD:628643. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77183 mRNA. Translation: AAA40723.1 .
    M84000 mRNA. Translation: AAA41591.1 .
    PIRi A42210.
    RefSeqi NP_665722.2. NM_145779.2.
    UniGenei Rn.11295.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EDY X-ray 2.30 A/B 1362-1495 [» ]
    ProteinModelPortali Q63041.
    SMRi Q63041. Positions 124-225, 1362-1495.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q63041. 1 interaction.
    STRINGi 10116.ENSRNOP00000009467.

    Proteomic databases

    PaxDbi Q63041.
    PRIDEi Q63041.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000009467 ; ENSRNOP00000009467 ; ENSRNOG00000006709 .
    GeneIDi 252922.
    KEGGi rno:252922.
    UCSCi RGD:628643. rat.

    Organism-specific databases

    CTDi 5858.
    RGDi 628643. Pzp.

    Phylogenomic databases

    eggNOGi COG2373.
    GeneTreei ENSGT00740000115177.
    HOGENOMi HOG000220939.
    HOVERGENi HBG000039.
    InParanoidi Q63041.
    OMAi THITNAF.
    OrthoDBi EOG7DJSKB.
    PhylomeDBi Q63041.
    TreeFami TF313285.

    Miscellaneous databases

    EvolutionaryTracei Q63041.
    NextBioi 624079.

    Gene expression databases

    Genevestigatori Q63041.

    Family and domain databases

    Gene3Di 1.50.10.20. 1 hit.
    2.60.40.690. 1 hit.
    InterProi IPR009048. A-macroglobulin_rcpt-bd.
    IPR011626. A2M_comp.
    IPR002890. A2M_N.
    IPR011625. A2M_N_2.
    IPR014756. Ig_E-set.
    IPR001599. Macroglobln_a2.
    IPR019742. MacrogloblnA2_CS.
    IPR019565. MacrogloblnA2_thiol-ester-bond.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    [Graphical view ]
    Pfami PF00207. A2M. 1 hit.
    PF07678. A2M_comp. 1 hit.
    PF01835. A2M_N. 1 hit.
    PF07703. A2M_N_2. 1 hit.
    PF07677. A2M_recep. 1 hit.
    PF10569. Thiol-ester_cl. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48239. SSF48239. 1 hit.
    SSF49410. SSF49410. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEi PS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of rat alpha 1-macroglobulin, a broad-range proteinase inhibitor from the alpha-macroglobulin-complement family."
      Eggertsen G., Hudson G., Shiels B., Reed D., Fey G.H.
      Mol. Biol. Med. 8:287-302(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-54; 724-743; 901-930 AND 1245-1269, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Strain: Fischer 344Imported.
      Tissue: LiverImported.
    2. "cDNA cloning and sequencing of rat alpha 1-macroglobulin."
      Warmegard B., Martin N., Johansson S.
      Biochemistry 31:2346-2352(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-DawleyImported.
      Tissue: LiverImported.
    3. Lubec G., Chen W.-Q.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1287-1294 AND 1321-1327, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Hippocampus.
    4. "Structure of a rat alpha 1-macroglobulin receptor-binding domain dimer."
      Xiao T., DeCamp D.L., Spran S.R.
      Protein Sci. 9:1889-1897(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1362-1495.

    Entry informationi

    Entry nameiA1M_RAT
    AccessioniPrimary (citable) accession number: Q63041
    Secondary accession number(s): Q63332
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 91 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3