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Protein

Macrophage mannose receptor 1

Gene

Mrc1

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

Functioni

Mediates the endocytosis of glycoproteins by macrophages. Binds both sulfated and non-sulfated polysaccharide chains. Acts as phagocytic receptor for bacteria, fungi and other pathogens.1 Publication

GO - Molecular functioni

  • mannose binding Source: MGI
  • receptor activity Source: UniProtKB
  • transmembrane signaling receptor activity Source: MGI

GO - Biological processi

  • cellular response to interferon-gamma Source: MGI
  • cellular response to interleukin-4 Source: MGI
  • cellular response to lipopolysaccharide Source: MGI
  • receptor-mediated endocytosis Source: UniProtKB
  • signal transduction Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Calcium, Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Macrophage mannose receptor 1
Short name:
MMR
Alternative name(s):
CD_antigen: CD206
Gene namesi
Name:Mrc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:97142. Mrc1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 13881369ExtracellularSequence analysisAdd
BLAST
Transmembranei1389 – 140921HelicalSequence analysisAdd
BLAST
Topological domaini1410 – 145647CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: MGI
  • endosome membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 14561437Macrophage mannose receptor 1PRO_0000017549Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi35 ↔ 49
Disulfide bondi74 ↔ 91
Disulfide bondi102 ↔ 149
Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence analysis
Disulfide bondi168 ↔ 194By similarity
Disulfide bondi182 ↔ 209By similarity
Disulfide bondi247 ↔ 340By similarity
Disulfide bondi316 ↔ 332By similarity
Glycosylationi344 – 3441N-linked (GlcNAc...)Sequence analysis
Disulfide bondi391 ↔ 486By similarity
Disulfide bondi463 ↔ 478By similarity
Glycosylationi529 – 5291N-linked (GlcNAc...)Sequence analysis
Disulfide bondi532 ↔ 625By similarity
Disulfide bondi600 ↔ 617By similarity
Disulfide bondi680 ↔ 777By similarity
Disulfide bondi753 ↔ 769By similarity
Disulfide bondi828 ↔ 922By similarity
Disulfide bondi899 ↔ 914By similarity
Glycosylationi926 – 9261N-linked (GlcNAc...)Sequence analysis
Glycosylationi930 – 9301N-linked (GlcNAc...)Sequence analysis
Disulfide bondi976 ↔ 1078By similarity
Disulfide bondi1051 ↔ 1070By similarity
Disulfide bondi1122 ↔ 1211By similarity
Glycosylationi1159 – 11591N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1189 ↔ 1203By similarity
Glycosylationi1204 – 12041N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1262 ↔ 1354By similarity
Disulfide bondi1331 ↔ 1346By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ61830.
MaxQBiQ61830.
PaxDbiQ61830.
PRIDEiQ61830.

PTM databases

PhosphoSiteiQ61830.

Expressioni

Tissue specificityi

Detected in macrophages.1 Publication

Inductioni

Down-regulated by interferon gamma.1 Publication

Gene expression databases

BgeeiQ61830.
CleanExiMM_MRC1.
ExpressionAtlasiQ61830. baseline and differential.
GenevisibleiQ61830. MM.

Interactioni

Protein-protein interaction databases

IntActiQ61830. 2 interactions.
MINTiMINT-1676071.
STRINGi10090.ENSMUSP00000028045.

Structurei

Secondary structure

1
1456
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 293Combined sources
Turni30 – 334Combined sources
Beta strandi34 – 407Combined sources
Beta strandi43 – 486Combined sources
Helixi54 – 563Combined sources
Beta strandi58 – 647Combined sources
Beta strandi66 – 683Combined sources
Turni69 – 724Combined sources
Beta strandi73 – 764Combined sources
Beta strandi78 – 803Combined sources
Beta strandi87 – 893Combined sources
Helixi96 – 983Combined sources
Beta strandi100 – 1023Combined sources
Beta strandi107 – 1104Combined sources
Beta strandi116 – 1183Combined sources
Helixi121 – 1233Combined sources
Beta strandi128 – 1314Combined sources
Helixi135 – 1373Combined sources
Beta strandi144 – 1474Combined sources
Helixi148 – 1514Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DQGX-ray1.70A20-154[»]
1DQOX-ray2.20A20-154[»]
1FWUX-ray1.90A21-154[»]
1FWVX-ray2.20A21-154[»]
ProteinModelPortaliQ61830.
SMRiQ61830. Positions 21-154, 161-211, 644-784.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ61830.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 142121Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST
Domaini163 – 21149Fibronectin type-IIPROSITE-ProRule annotationAdd
BLAST
Domaini225 – 341117C-type lectin 1PROSITE-ProRule annotationAdd
BLAST
Domaini369 – 487119C-type lectin 2PROSITE-ProRule annotationAdd
BLAST
Domaini511 – 626116C-type lectin 3PROSITE-ProRule annotationAdd
BLAST
Domaini655 – 778124C-type lectin 4PROSITE-ProRule annotationAdd
BLAST
Domaini807 – 923117C-type lectin 5PROSITE-ProRule annotationAdd
BLAST
Domaini951 – 1079129C-type lectin 6PROSITE-ProRule annotationAdd
BLAST
Domaini1101 – 1212112C-type lectin 7PROSITE-ProRule annotationAdd
BLAST
Domaini1240 – 1355116C-type lectin 8PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 8 C-type lectin domains.PROSITE-ProRule annotation
Contains 1 fibronectin type-II domain.PROSITE-ProRule annotation
Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IS47. Eukaryota.
ENOG410XRS3. LUCA.
GeneTreeiENSGT00720000108514.
HOGENOMiHOG000113647.
HOVERGENiHBG107130.
InParanoidiQ61830.
KOiK06560.
OMAiCYMIGHT.
OrthoDBiEOG7FFMQR.
TreeFamiTF316663.

Family and domain databases

Gene3Di2.10.10.10. 1 hit.
3.10.100.10. 8 hits.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR000562. FN_type2_col-bd.
IPR013806. Kringle-like.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00040. fn2. 1 hit.
PF00059. Lectin_C. 8 hits.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 8 hits.
SM00059. FN2. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF56436. SSF56436. 8 hits.
SSF57440. SSF57440. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 6 hits.
PS50041. C_TYPE_LECTIN_2. 8 hits.
PS00023. FN2_1. 1 hit.
PS51092. FN2_2. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q61830-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLLLLLAFI SVIPVSVQLL DARQFLIYNE DHKRCVDALS AISVQTATCN
60 70 80 90 100
PEAESQKFRW VSDSQIMSVA FKLCLGVPSK TDWASVTLYA CDSKSEYQKW
110 120 130 140 150
ECKNDTLFGI KGTELYFNYG NRQEKNIKLY KGSGLWSRWK VYGTTDDLCS
160 170 180 190 200
RGYEAMYSLL GNANGAVCAF PFKFENKWYA DCTSAGRSDG WLWCGTTTDY
210 220 230 240 250
DKDKLFGFCP LHFEGSERLW NKDPLTGILY QINSKSALTW HQARASCKQQ
260 270 280 290 300
NADLLSVTEI HEQMYLTGLT SSLSSGLWIG LNSLSVRSGW QWAGGSPFRY
310 320 330 340 350
LNWLPGSPSS EPGKSCVSLN PGKNAKWENL ECVQKLGYIC KKGNNTLNPF
360 370 380 390 400
IIPSASDVPT GCPNQWWPYA GHCYRIHREE KKIQKYALQA CRKEGGDLAS
410 420 430 440 450
IHSIEEFDFI FSQLGYEPND ELWIGLNDIK IQMYFEWSDG TPVTFTKWLP
460 470 480 490 500
GEPSHENNRQ EDCVVMKGKD GYWADRACEQ PLGYICKMVS QSHAVVPEGA
510 520 530 540 550
DKGCRKGWKR HGFYCYLIGS TLSTFTDANH TCTNEKAYLT TVEDRYEQAF
560 570 580 590 600
LTSLVGLRPE KYFWTGLSDV QNKGTFRWTV DEQVQFTHWN ADMPGRKAGC
610 620 630 640 650
VAMKTGVAGG LWDVLSCEEK AKFVCKHWAE GVTRPPEPTT TPEPKCPENW
660 670 680 690 700
GTTSKTSMCF KLYAKGKHEK KTWFESRDFC KAIGGELASI KSKDEQQVIW
710 720 730 740 750
RLITSSGSYH ELFWLGLTYG SPSEGFTWSD GSPVSYENWA YGEPNNYQNV
760 770 780 790 800
EYCGELKGDP GMSWNDINCE HLNNWICQIQ KGKTLLPEPT PAPQDNPPVT
810 820 830 840 850
ADGWVIYKDY QYYFSKEKET MDNARAFCKK NFGDLATIKS ESEKKFLWKY
860 870 880 890 900
INKNGGQSPY FIGMLISMDK KFIWMDGSKV DFVAWATGEP NFANDDENCV
910 920 930 940 950
TMYTNSGFWN DINCGYPNNF ICQRHNSSIN ATAMPTTPTT PGGCKEGWHL
960 970 980 990 1000
YKNKCFKIFG FANEEKKSWQ DARQACKGLK GNLVSIENAQ EQAFVTYHMR
1010 1020 1030 1040 1050
DSTFNAWTGL NDINAEHMFL WTAGQGVHYT NWGKGYPGGR RSSLSYEDAD
1060 1070 1080 1090 1100
CVVVIGGNSR EAGTWMDDTC DSKQGYICQT QTDPSLPVSP TTTPKDGFVT
1110 1120 1130 1140 1150
YGKSSYSLMK LKLPWHEAET YCKDHTSLLA SILDPYSNAF AWMKMHPFNV
1160 1170 1180 1190 1200
PIWIALNSNL TNNEYTWTDR WRVRYTNWGA DEPKLKSACV YMDVDGYWRT
1210 1220 1230 1240 1250
SYCNESFYFL CKKSDEIPAT EPPQLPGKCP ESEQTAWIPF YGHCYYFESS
1260 1270 1280 1290 1300
FTRSWGQASL ECLRMGASLV SIETAAESSF LSYRVEPLKS KTNFWIGMFR
1310 1320 1330 1340 1350
NVEGKWLWLN DNPVSFVNWK TGDPSGERND CVVLASSSGL WNNIHCSSYK
1360 1370 1380 1390 1400
GFICKMPKII DPVTTHSSIT TKADQRKMDP QPKGSSKAAG VVTVVLLIVI
1410 1420 1430 1440 1450
GAGVAAYFFY KKRHALHIPQ EATFENTLYF NSNLSPGTSD TKDLMGNIEQ

NEHAII
Length:1,456
Mass (Da):164,981
Last modified:July 27, 2011 - v2
Checksum:iFD568C1B812214D2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti826 – 8261A → R in CAA78028 (PubMed:1421407).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11974 mRNA. Translation: CAA78028.1.
AL845290 Genomic DNA. No translation available.
AL845434 Genomic DNA. No translation available.
AK079897 mRNA. Translation: BAC37778.1.
CCDSiCCDS15700.1.
PIRiA48925.
RefSeqiNP_032651.2. NM_008625.2.
UniGeneiMm.2019.

Genome annotation databases

EnsembliENSMUST00000028045; ENSMUSP00000028045; ENSMUSG00000026712.
GeneIDi17533.
KEGGimmu:17533.
UCSCiuc008ikk.2. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Macrophage mannose receptor

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11974 mRNA. Translation: CAA78028.1.
AL845290 Genomic DNA. No translation available.
AL845434 Genomic DNA. No translation available.
AK079897 mRNA. Translation: BAC37778.1.
CCDSiCCDS15700.1.
PIRiA48925.
RefSeqiNP_032651.2. NM_008625.2.
UniGeneiMm.2019.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DQGX-ray1.70A20-154[»]
1DQOX-ray2.20A20-154[»]
1FWUX-ray1.90A21-154[»]
1FWVX-ray2.20A21-154[»]
ProteinModelPortaliQ61830.
SMRiQ61830. Positions 21-154, 161-211, 644-784.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ61830. 2 interactions.
MINTiMINT-1676071.
STRINGi10090.ENSMUSP00000028045.

PTM databases

PhosphoSiteiQ61830.

Proteomic databases

EPDiQ61830.
MaxQBiQ61830.
PaxDbiQ61830.
PRIDEiQ61830.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028045; ENSMUSP00000028045; ENSMUSG00000026712.
GeneIDi17533.
KEGGimmu:17533.
UCSCiuc008ikk.2. mouse.

Organism-specific databases

CTDi4360.
MGIiMGI:97142. Mrc1.

Phylogenomic databases

eggNOGiENOG410IS47. Eukaryota.
ENOG410XRS3. LUCA.
GeneTreeiENSGT00720000108514.
HOGENOMiHOG000113647.
HOVERGENiHBG107130.
InParanoidiQ61830.
KOiK06560.
OMAiCYMIGHT.
OrthoDBiEOG7FFMQR.
TreeFamiTF316663.

Miscellaneous databases

EvolutionaryTraceiQ61830.
PROiQ61830.
SOURCEiSearch...

Gene expression databases

BgeeiQ61830.
CleanExiMM_MRC1.
ExpressionAtlasiQ61830. baseline and differential.
GenevisibleiQ61830. MM.

Family and domain databases

Gene3Di2.10.10.10. 1 hit.
3.10.100.10. 8 hits.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR000562. FN_type2_col-bd.
IPR013806. Kringle-like.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00040. fn2. 1 hit.
PF00059. Lectin_C. 8 hits.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 8 hits.
SM00059. FN2. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF56436. SSF56436. 8 hits.
SSF57440. SSF57440. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 6 hits.
PS50041. C_TYPE_LECTIN_2. 8 hits.
PS00023. FN2_1. 1 hit.
PS51092. FN2_2. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the murine macrophage mannose receptor: demonstration that the downregulation of receptor expression mediated by interferon-gamma occurs at the level of transcription."
    Harris N., Rits M., Chang G., Ezekowitz R.A.B.
    Blood 80:2363-2373(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
    Strain: C57BL/6J.
    Tissue: Macrophage.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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] OF 1318-1456.
    Strain: C57BL/6J.
    Tissue: Thymus.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "Crystal structure of the cysteine-rich domain of mannose receptor complexed with a sulfated carbohydrate ligand."
    Liu Y., Chirino A.J., Misulovin Z., Leteux C., Feizi T., Nussenzweig M.C., Bjorkman P.J.
    J. Exp. Med. 191:1105-1116(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 20-153 IN COMPLEX WITH CARBOHYDRATE LIGAND.
  6. "The molecular mechanism of sulfated carbohydrate recognition by the cysteine-rich domain of mannose receptor."
    Liu Y., Misulovin Z., Bjorkman P.J.
    J. Mol. Biol. 305:481-490(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 21-154 IN COMPLEX WITH CARBOHYDRATE LIGAND.

Entry informationi

Entry nameiMRC1_MOUSE
AccessioniPrimary (citable) accession number: Q61830
Secondary accession number(s): Q8C502
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.