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
//