CPLM-014628

CPLM 1.0 - Compendium of Protein Lysine Modification

Tag

Content

CPLM ID

CPLM-014628

UniProt Accession

MRC2_MOUSE; Q64449; A2AAB0; Q6ZQ64; Q8C6P0

Genbank Protein ID

U56734; AK054150; AL645684; AL645471; AL645572; AL645572; AL645471; AL645684; AL645471; AL645572; AL645684; AK129195

Genbank Nucleotide ID

AAC52729.1; BAC35672.1; CAM22193.1; CAM22193.1; CAM22193.1; CAM22804.1; CAM22804.1; CAM22804.1; CAM24832.1; CAM24832.1; CAM24832.1; BAC98005.1

Protein Name

C-type mannose receptor 2

Protein Synonyms/Alias

Lectin lambda; Macrophage mannose receptor 2; CD280

Gene Name

Mrc2

Gene Synonyms/Alias

Kiaa0709

Created Date

July 27, 2013

Organism

Mus musculus (Mouse)

NCBI Taxa ID

10090

Lysine Modification

Position	Peptide	Type	References
1146	LQKPLRWKDALLLCE	acetylation	[1]
1236	RTTSCDTKLQGAVCG	acetylation	[1]

Reference

[1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]

Functional Description

May play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. Internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. May be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. May contribute to cellular uptake, remodeling and degradation of extracellular collagen matrices. May participate in remodeling of extracellular matrix co-operating with the matrix metalloproteinases (MMPs).

Sequence Annotation

DOMAIN 37 190 Ricin B-type lectin.
DOMAIN 181 229 Fibronectin type-II.
DOMAIN 243 359 C-type lectin 1.
DOMAIN 388 504 C-type lectin 2.
DOMAIN 527 643 C-type lectin 3.
DOMAIN 677 808 C-type lectin 4.
DOMAIN 831 950 C-type lectin 5.
DOMAIN 978 1106 C-type lectin 6.
DOMAIN 1131 1242 C-type lectin 7.
DOMAIN 1271 1391 C-type lectin 8.
CARBOHYD 101 101 N-linked (GlcNAc...) (Potential).
CARBOHYD 139 139 N-linked (GlcNAc...).
CARBOHYD 363 363 N-linked (GlcNAc...).
CARBOHYD 1028 1028 N-linked (GlcNAc...) (Potential).
CARBOHYD 1348 1348 N-linked (GlcNAc...) (Potential).
DISULFID 92 111 By similarity.
DISULFID 186 212 By similarity.
DISULFID 200 227 By similarity.
DISULFID 265 358 By similarity.
DISULFID 334 350 By similarity.
DISULFID 409 503 By similarity.
DISULFID 480 495 By similarity.
DISULFID 617 634 By similarity.
DISULFID 703 807 By similarity.
DISULFID 784 799 By similarity.
DISULFID 852 949 By similarity.
DISULFID 926 941 By similarity.
DISULFID 1077 1097 By similarity.
DISULFID 1219 1233 By similarity.
DISULFID 1367 1382 By similarity.
CROSSLNK 1141 1141 Glycyl lysine isopeptide (Lys-Gly)

Keyword

Alternative splicing; Calcium; Complete proteome; Disulfide bond; Endocytosis; Glycoprotein; Isopeptide bond; Lectin; Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix; Ubl conjugation.

Sequence Source

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

Protein Length

1479 AA

Protein Sequence

MVPIRPALAP WPRHLLRCVL LLGGLRLGHP ADSAAALLEP DVFLIFSQGM QGCLEAQGVQ 60
VRVTPVCNAS LPAQRWKWVS RNRLFNLGAT QCLGTGWPVT NTTVSLGMYE CDREALSLRW 120
QCRTLGDQLS LLLGARASNA SKPGTLERGD QTRSGHWNIY GSEEDLCARP YYEVYTIQGN 180
SHGKPCTIPF KYDNQWFHGC TSTGREDGHL WCATTQDYGK DERWGFCPIK SNDCETFWDK 240
DQLTDSCYQF NFQSTLSWRE AWASCEQQGA DLLSITEIHE QTYINGLLTG YSSTLWIGLN 300
DLDTSGGWQW SDNSPLKYLN WESDQPDNPG EENCGVIRTE SSGGWQNHDC SIALPYVCKK 360
KPNATVEPIQ PDRWTNVKVE CDPSWQPFQG HCYRLQAEKR SWQESKRACL RGGGDLLSIH 420
SMAELEFITK QIKQEVEELW IGLNDLKLQM NFEWSDGSLV SFTHWHPFEP NNFRDSLEDC 480
VTIWGPEGRW NDSPCNQSLP SICKKAGRLS QGAAEEDHGC RKGWTWHSPS CYWLGEDQVI 540
YSDARRLCTD HGSQLVTITN RFEQAFVSSL IYNWEGEYFW TALQDLNSTG SFRWLSGDEV 600
IYTHWNRDQP GYRRGGCVAL ATGSAMGLWE VKNCTSFRAR YICRQSLGTP VTPELPGPDP 660
TPSLTGSCPQ GWVSDPKLRH CYKVFSSERL QEKKSWIQAL GVCRELGAQL LSLASYEEEH 720
FVAHMLNKIF GESEPESHEQ HWFWIGLNRR DPREGHSWRW SDGLGFSYHN FARSRHDDDD 780
IRGCAVLDLA SLQWVPMQCQ TQLDWICKIP RGVDVREPDI GRQGRLEWVR FQEAEYKFFE 840
HHSSWAQAQR ICTWFQADLT SVHSQAELDF LGQNLQKLSS DQEQHWWIGL HTLESDGRFR 900
WTDGSIINFI SWAPGKPRPI GKDKKCVYMT ARQEDWGDQR CHTALPYICK RSNSSGETQP 960
QDLPPSALGG CPSGWNQFLN KCFRIQGQDP QDRVKWSEAQ FSCEQQEAQL VTIANPLEQA 1020
FITASLPNVT FDLWIGLHAS QRDFQWIEQE PLLYTNWAPG EPSGPSPAPS GTKPTSCAVI 1080
LHSPSAHFTG RWDDRSCTEE THGFICQKGT DPSLSPSPAA TPPAPGAELS YLNHTFRLLQ 1140
KPLRWKDALL LCESRNASLA HVPDPYTQAF LTQAARGLQT PLWIGLASEE GSRRYSWLSE 1200
EPLNYVSWQD EEPQHSGGCA YVDVDGTWRT TSCDTKLQGA VCGVSRGPPP RRINYRGSCP 1260
QGLADSSWIP FREHCYSFHM EVLLGHKEAL QRCQKAGGTV LSILDEMENV FVWEHLQTAE 1320
AQSRGAWLGM NFNPKGGTLV WQDNTAVNYS NWGPPGLGPS MLSHNSCYWI QSSSGLWRPG 1380
ACTNITMGVV CKLPRVEENS FLPSAALPES PVALVVVLTA VLLLLALMTA ALILYRRRQS 1440
AERGSFEGAR YSRSSHSGPA EATEKNILVS DMEMNEQQE 1479

Gene Ontology

GO:0009986; C:cell surface; ISA:MGI.
GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
GO:0005886; C:plasma membrane; TAS:Reactome.
GO:0030246; F:carbohydrate binding; ISA:MGI.
GO:0005518; F:collagen binding; ISA:MGI.
GO:0006897; P:endocytosis; IEA:UniProtKB-KW.

Interpro

IPR001304; 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.

Pfam

PF00040; fn2
PF00059; Lectin_C

SMART

SM00034; CLECT
SM00059; FN2
SM00458; RICIN

PROSITE

PS00615; C_TYPE_LECTIN_1
PS50041; C_TYPE_LECTIN_2
PS00023; FN2_1
PS51092; FN2_2
PS50231; RICIN_B_LECTIN

PRINTS