ID   TETN_BOVIN              Reviewed;         202 AA.
AC   Q2KIS7;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Tetranectin;
DE            Short=TN;
DE   AltName: Full=C-type lectin domain family 3 member B;
DE   Flags: Precursor;
GN   Name=CLEC3B;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
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DR   EMBL; BC112525; AAI12526.1; -; mRNA.
DR   RefSeq; NP_001039677.1; NM_001046212.1.
DR   AlphaFoldDB; Q2KIS7; -.
DR   SMR; Q2KIS7; -.
DR   STRING; 9913.ENSBTAP00000024391; -.
DR   PaxDb; Q2KIS7; -.
DR   PeptideAtlas; Q2KIS7; -.
DR   PRIDE; Q2KIS7; -.
DR   GeneID; 515783; -.
DR   KEGG; bta:515783; -.
DR   CTD; 7123; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   HOGENOM; CLU_049894_6_1_1; -.
DR   InParanoid; Q2KIS7; -.
DR   OrthoDB; 1236353at2759; -.
DR   TreeFam; TF330481; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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; IEA:UniProtKB-KW.
DR   GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR   GO; GO:0030282; P:bone mineralization; IEP:UniProtKB.
DR   GO; GO:0001503; P:ossification; IBA:GO_Central.
DR   GO; GO:0010756; P:positive regulation of plasminogen activation; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Disulfide bond; Lectin; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..202
FT                   /note="Tetranectin"
FT                   /id="PRO_0000240304"
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"
SQ   SEQUENCE   202 AA;  22144 MW;  23B8AB5E30BE6DCA CRC64;
     MELWGPCVLL CLFSLLTQVT AETPTPKAKK AANAKKDAVS PKMLEELKTQ LDSLAQEVAL
     LKEQQALQTV CLKGTKVHMK CFLAFVQAKT FHEASEDCIS RGGTLGTPQT GSENDALYEY
     LRQSVGSEAE VWLGFNDMAS EGSWVDMTGG HIAYKNWETE ITAQPDGGKV ENCATLSGAA
     NGKWFDKRCR DKLPYVCQFA IV