GenomeNet

Database: UniProt
Entry: G9L057_MUSPF
LinkDB: G9L057_MUSPF
Original site: G9L057_MUSPF 
ID   G9L057_MUSPF            Unreviewed;       503 AA.
AC   G9L057;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   SubName: Full=Chondroitin sulfate proteoglycan 2 {ECO:0000313|EMBL:AES10536.1};
DE   Flags: Fragment;
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|EMBL:AES10536.1};
RN   [1] {ECO:0000313|EMBL:AES10536.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Lungs {ECO:0000313|EMBL:AES10536.1};
RX   PubMed=23236062; DOI=10.1128/JVI.02476-12;
RA   Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F.,
RA   Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., Ross T.M.,
RA   Farooqui A., Kelvin D.J.;
RT   "Sequencing, annotation, and characterization of the influenza ferret
RT   infectome.";
RL   J. Virol. 87:1957-1966(2013).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; JP021938; AES10536.1; -; mRNA.
DR   AlphaFoldDB; G9L057; -.
DR   HOGENOM; CLU_000303_1_1_1; -.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   CDD; cd00033; CCP; 1.
DR   CDD; cd00054; EGF_CA; 2.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 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   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   PANTHER; PTHR45836; SLIT HOMOLOG; 1.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF00084; Sushi; 1.
DR   PRINTS; PR00010; EGFBLOOD.
DR   SMART; SM00032; CCP; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 2.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50923; SUSHI; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Lectin {ECO:0000256|ARBA:ARBA00022734};
KW   Sushi {ECO:0000256|PROSITE-ProRule:PRU00302}.
FT   DOMAIN          223..259
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          261..297
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          310..424
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          428..488
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   REGION          23..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        249..258
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        287..296
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        430..473
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        459..486
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AES10536.1"
FT   NON_TER         503
FT                   /evidence="ECO:0000313|EMBL:AES10536.1"
SQ   SEQUENCE   503 AA;  56187 MW;  50F35DF166EE7E81 CRC64;
     SPGSLADMEV TFTSLNEELL HITEPPSLSP DTGLEPSEDE SHPKLLEQME ASSTELTAEE
     GTEILQDSQT QANIQLSGEI MTSNIRTPEP GTMVTTAGES KLEGATPWPH STSASAIYGV
     EADVVPQPSP QTSEWPTVPS SLEINPETHT ALIRGEDHTV PTSEQQVTTR ILDSNNQATV
     SIAELNTELP TPSFSLLETS NETGFLIGIN EESVEGTAVY LPGPDRCKTN PCLNGGTCYP
     TDTSYVCTCV PGFSGDQCEL DFDECHSNPC RNGATCVDGF NTFRCLCLPS YVGALCEQDT
     ETCDYGWHKF QGQCYKYFAH RRTWDAAERE CRLQGAHLTS ILSHEEQMFV NRVGHDYQWI
     GLNDKMFEHD FRWTDGSTLQ YENWRPNQPD SFFSAGEDCV VIIWHENGQW NDVPCNYHLT
     YTCKKGTVAC GQPPVVENAK TFGKMKPRYE INSLIRYHCK DGFIQRHLPT IRCLGNGRWA
     MPKITCMNPS AYQRTYSKKY FKN
//
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