ID C3ZPL6_BRAFL Unreviewed; 1143 AA.
AC C3ZPL6;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=C-type lectin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BRAFLDRAFT_88361 {ECO:0000313|EMBL:EEN45513.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN45513.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN45513.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN45513.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the thrombospondin family.
CC {ECO:0000256|ARBA:ARBA00009456}.
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; GG666658; EEN45513.1; -; Genomic_DNA.
DR RefSeq; XP_002589502.1; XM_002589456.1.
DR AlphaFoldDB; C3ZPL6; -.
DR eggNOG; KOG4441; Eukaryota.
DR InParanoid; C3ZPL6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00037; CLECT; 1.
DR CDD; cd00054; EGF_CA; 2.
DR Gene3D; 1.25.40.420; -; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 4.10.1080.10; TSP type-3 repeat; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR000210; BTB/POZ_dom.
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; IPR013320; ConA-like_dom_sf.
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; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR InterPro; IPR017897; Thrombospondin_3_rpt.
DR InterPro; IPR008859; Thrombospondin_C.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR PANTHER; PTHR10199:SF100; THROMBOSPONDIN, ISOFORM A; 1.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF07699; Ephrin_rec_like; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF02412; TSP_3; 2.
DR Pfam; PF05735; TSP_C; 2.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM01411; Ephrin_rec_like; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF54695; POZ domain; 1.
DR SUPFAM; SSF103647; TSP type-3 repeat; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50923; SUSHI; 1.
DR PROSITE; PS51234; TSP3; 1.
DR PROSITE; PS51236; TSP_CTER; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00634}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 374..497
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 539..581
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 578..654
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REPEAT 950..985
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 981..1141
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
SQ SEQUENCE 1143 AA; 126153 MW; A8BF0859376EAB80 CRC64;
MAHHHYCYII WVISVCLVSV PFDLGFMPSI STWLPHTQNP TSAQFVLVPT KMRAICTDFL
KLWTTYKRLG YCRMSSLKSR AASFPAIGLL CPRPAPTSEI LHMGATLTAG HIICKTITGL
DANIFGEILS YIYSGTLHVS LDKVQPLYQA ADLLQLNYVR NTCSSYMTMN VECSTCVDLY
KFADFFALVV SSKEFCSLSV NQLTEIISHD ELDVKEETTV WEAVVRWVQH SREERLHHLP
SILSHIRFNL LSSDYTAAIL EHPLVKEDPG SSEVIRNIMV QERNHDVKPG PEVTMEMALL
FDTGRRYADT WRDLEANLSD STRVPRGFEC PVAHEYILNA LGFDSAVEGR FIATRHGHQP
HLWEAHSGNQ HRDLDGYRYQ TFTTYLNYDQ AQATCVSNGG HLAHIKSSRQ QSVLANMATL
TAGWGSDYWI GLTDRQSEGI WRWTDGTGLN YRNWAEGEPT NGNAVDGEQD CVALWGDYGY
THWDDRQCGH WLYFICQTDK NECSNNNGGC DQICHNTAGG YHCSCNAGYQ LSGSSQCDDI
DECLTNGGRG PCDQTCTNLV GSYRCSCTVG YQLDADSVSC SEPCSEAFAP PLNGGKACSV
TDDTTGGMFC TVYCHEDKEF AIAPAQAYTC RADGRWFADS NLVVEPTPWP DCTGRYRPGR
PHMLGELHYF SGTDCSSSRD EIISKFQQLF NQMDSSQPGG NMTIELQNVE VVCGATSRQA
TSKRGQKFIS KSERSANGFT VKFMVVAISS LAPADVTETV QADLVYALDD VYFDIEDKVA
SQQFDLNVNG QQATVDTFDI GFAEFDLNCT QGQLSFQDSF EAYCLDCPLG TFHDLTTDTC
EYCPVGEYQN HPVQTACKPC PVNTWSVFPG AKEEAQCMSV CLGKDDLCSS CVHVKGQLTR
KCEVGWAGSQ DGLTCGLDGD QDGYPIAPLS CNGTGCKKDN CPGIPNSGQE DTDGDGMGDT
CDDDMDNDVF LNVEDNCPLT MNVNQTDSDR DGVGDVCDNC PADFNTDQRD TDGDGVGDVC
DSDADSDGPD YFGNLDYSGT FFVNTQTDDD FVGFVFSYQS NSRFYLVSWK QTGDSQGGQA
GVQLKIPPVR RFHLYEGSRT VVDSGDVQDA SLRGGRLGVY CYSQENVIWS HLVTKCDGNI
PSA
//
