TETN_MOUSE
ID TETN_MOUSE Reviewed; 202 AA.
AC P43025;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Tetranectin;
DE Short=TN;
DE AltName: Full=C-type lectin domain family 3 member B;
DE AltName: Full=Plasminogen kringle 4-binding protein;
DE Flags: Precursor;
GN Name=Clec3b; Synonyms=Tna;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Lung;
RX PubMed=7835708; DOI=10.1016/0378-1119(94)00703-u;
RA Soerensen C.B., Berglund L., Petersen T.E.;
RT "Cloning of a cDNA encoding murine tetranectin.";
RL Gene 152:243-245(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=8563165; DOI=10.1007/bf00354289;
RA Ibaraki K., Kozak C.A., Wewer U.M., Albrechtsen R., Young M.F.;
RT "Mouse tetranectin: cDNA sequence, tissue-specific expression, and
RT chromosomal mapping.";
RL Mamm. Genome 6:693-696(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=9409787; DOI=10.1016/s0378-1119(97)00451-4;
RA Soerensen C.B., Berglund L., Petersen T.E.;
RT "Cloning of the murine tetranectin gene and 5'-flanking region.";
RL Gene 201:199-202(1997).
RN [4]
RP PROTEIN SEQUENCE OF 28-35, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Tetranectin binds to plasminogen and to isolated kringle 4.
CC May be involved in the packaging of molecules destined for exocytosis
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Highest expression in lung and skeletal muscle.
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DR EMBL; X79199; CAA55791.1; -; mRNA.
DR EMBL; U08595; AAA96811.1; -; mRNA.
DR EMBL; X98122; CAA66804.1; -; Genomic_DNA.
DR CCDS; CCDS23656.1; -.
DR PIR; JC4031; JC4031.
DR AlphaFoldDB; P43025; -.
DR SMR; P43025; -.
DR STRING; 10090.ENSMUSP00000026890; -.
DR MaxQB; P43025; -.
DR PaxDb; P43025; -.
DR PeptideAtlas; P43025; -.
DR PRIDE; P43025; -.
DR ProteomicsDB; 259003; -.
DR MGI; MGI:104540; Clec3b.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; P43025; -.
DR PhylomeDB; P43025; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR ChiTaRS; Clec3b; mouse.
DR PRO; PR:P43025; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P43025; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; TAS:MGI.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0001652; C:granular component; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; TAS:MGI.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0036143; F:kringle domain binding; ISO:MGI.
DR GO; GO:0030282; P:bone mineralization; ISS:UniProtKB.
DR GO; GO:0001503; P:ossification; IEP:UniProtKB.
DR GO; GO:0010756; P:positive regulation of plasminogen activation; IDA:UniProtKB.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Lectin; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..202
FT /note="Tetranectin"
FT /id="PRO_0000017472"
FT DOMAIN 77..198
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 71..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 98..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 173..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 19..20
FT /note="LT -> VI (in Ref. 2; AAA96811)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="A -> T (in Ref. 2; AAA96811)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="A -> R (in Ref. 2; AAA96811)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="R -> Q (in Ref. 2; AAA96811)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 22257 MW; 639E7334D58EB04E CRC64;
MGFWGTYLLF CLFSFLSQLT AESPTPKAKK AANAKKDLVS SKMFEELKNR MDVLAQEVAL
LKEKQALQTV CLKGTKVNLK CLLAFTQPKT FHEASEDCIS QGGTLGTPQS ELENEALFEY
ARHSVGNDAN IWLGLNDMAA EGAWVDMTGG LLAYKNWETE ITTQPDGGKA ENCAALSGAA
NGKWFDKRCR DQLPYICQFA IV
