ID A0AA89C118_PINIB Unreviewed; 2115 AA.
AC A0AA89C118;
DT 27-MAR-2024, integrated into UniProtKB/TrEMBL.
DT 27-MAR-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE RecName: Full=C-type lectin domain-containing protein {ECO:0000259|PROSITE:PS50041};
GN ORFNames=FSP39_010172 {ECO:0000313|EMBL:KAK3090222.1};
OS Pinctada imbricata (Atlantic pearl-oyster) (Pinctada martensii).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada.
OX NCBI_TaxID=66713 {ECO:0000313|EMBL:KAK3090222.1, ECO:0000313|Proteomes:UP001186944};
RN [1] {ECO:0000313|EMBL:KAK3090222.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ZZ-2019 {ECO:0000313|EMBL:KAK3090222.1};
RC TISSUE=Adductor muscle {ECO:0000313|EMBL:KAK3090222.1};
RA Zheng Z.;
RT "The improved chromosome-level genome for the pearl oyster Pinctada fucata
RT martensii using PacBio sequencing and Hi-C.";
RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FRAS1 family.
CC {ECO:0000256|ARBA:ARBA00005529}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAK3090222.1}.
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DR EMBL; VSWD01000010; KAK3090222.1; -; Genomic_DNA.
DR Proteomes; UP001186944; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR CDD; cd00037; CLECT; 1.
DR Gene3D; 2.60.40.2030; -; 1.
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; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR039005; CSPG_rpt.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR045658; FRAS1-rel_N.
DR InterPro; IPR051561; FRAS1_ECM.
DR PANTHER; PTHR45739:SF11; FRAS1-RELATED EXTRACELLULAR MATRIX PROTEIN 1-LIKE ISOFORM X1; 1.
DR PANTHER; PTHR45739; MATRIX PROTEIN, PUTATIVE-RELATED; 1.
DR Pfam; PF16184; Cadherin_3; 11.
DR Pfam; PF03160; Calx-beta; 1.
DR Pfam; PF19309; Frem_N; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00237; Calx_beta; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF141072; CalX-like; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS51854; CSPG; 11.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP001186944};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..2115
FT /note="C-type lectin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041743176"
FT REPEAT 259..355
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT REPEAT 380..467
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT REPEAT 488..582
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT REPEAT 609..721
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT REPEAT 743..834
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT REPEAT 855..949
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT REPEAT 1070..1167
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT REPEAT 1188..1292
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT REPEAT 1313..1405
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT REPEAT 1427..1516
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT REPEAT 1547..1644
FT /note="CSPG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01201"
FT DOMAIN 1966..2078
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 1812..1899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2087..2115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1812..1830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1837..1847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1853..1880
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1888..1899
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2115 AA; 238638 MW; 22CCFCFB32DFC569 CRC64;
MKEIFGNLLC LLFFYVASGQ LLLVSKKEVT VKIGRDVYLK RDDLVFTKTT KGEECRVEVV
QNDPITQRVG YLEPQIFDCS FLPHTVHYVH NGSPLLQEDQ VRLRVHKFTH VATVSETFLL
DIRVDNSSHS AVITRGLRSV IVPEFNGISN TIDSSVIRFH HSGNQNVSCT VSFSKYKSVW
PLAGQIVIGN RRQNVEALKK SCRDFLYSNL HYQHTKSPSP NVDYLPLTIE LYDPSISDEV
KVERYFLPIH IKGALQNSPP RSSFMSMYMM DVDQFVLSTI IPGVISAEDF ETNSIQLVYN
ISKMPRNADG YFVNLKDHTT PIYSFLQDDL ENHRIAFQPP SYSISQRHVF DTEFTVYDSH
FVSSTPIVLH IAVRPSRTNG PRVSYNKGLV LLEGQERPLT TNSLKIVDSD NLEKVRLYVT
GGLQHGRLEK NSRRAIALTV QDLQQGSVRY IHDDSDSMKD QIDFRVSDGV NTVVINFPID
IIPKDDTAPY IVNNLGIEVN EGEMKRITSS MLMAHDIDSV DRNIEYLISQ PPSAGEIIKR
QKSSNTGTRV NKFKQRDIQK GLIFYRHFGH EEFKDLFTFK LRDQQRPPNE SDLETFHILI
NPVHENPPQL APDATRLVHV LETDVAFITK AELQYTDVET DDNQLSYMIT SAPYFVYNTG
NEDAGKIIAT HNISSVTKDG SLPAIQTFKQ EDINHMKIAY MPPMSDIGPE SRLVRFVYTV
QDSSGNKVLG QYFEIDVQPV NDKPPVFITS KLLVEEGGIL GLSTNQLSAS DEDTLPADLV
FILDERPAFG VMQKGGNALN EGDMFKLEDL RRKDIRYIHD GADVVLDTFT VTVSDGVNRA
SKVLSVDIVP IDDKAPHLKS NLRPRLIVSE GGSAIITSSV LAATDDDTDD HQLVFLIVKQ
PNHGIMQLGN QPATKFTQKN VEERRVRYIH TGGEIGNTVV RDTVTFIVSD QNYLATSDLP
VYDLNITITP VDNSKPIIIT GQELAVNESS KISLTPAVIT AKDPDTDPDE IRFIVLRHPQ
WGYLENSKTE SSNHRGVEPV YDEVQLYATD GKQRSTPETL RIKIKPFNDE EPDVMLQGFN
LDEGGQKVID QSMVDALDMD FPKDVLTFSI SQAPKHGEIV IMLHTRNGDV EAAIQDFTAE
ELHAGMKLKY KHDNSENFRD NFAVTVSDGK HQVKKMCNIS INPLNDEGPE VTKNAGLQLE
YGDYAMISSV VLQSIDPDNS ENEVFYILVS VPKKGSLQFC SDPFSPTRAS ECSDMHVGNN
FTQHDIDMNR IRYIHTTSMG STETDSFLFL LSDGTNRRQV ETFEIRIRNS RKANLALLNK
GLQVREGQRT PLSTDNLSAT DESTKADEIV FAITRQPNLG QMEFIDEPLK IIRSFTQLDI
ASRKVVYNHM TKSDITTDSF AFTVTNGLSQ AKDGVFKISI DPLDTILPSL QVNSLIEVLQ
GSDIEISPQH LLSQDPDTPD VNVTYVLAKP PTYGRLFNRG IAITRTFTQS EINLGFIVYE
SDGSHAGLDN FLFTLSDGKH DGFLVNSTLQ LKPVICSIFI KPVVNDAPKL LVSSHPETLE
YFGRDRYGFR LNSRNLKAID SDTSNSKLKY VMVKRPSHGH IENVATKRFV RRRFSQKDLD
DNNLLYILDK RRGATNDSFK FRLIDGRGNT LDNLRFDMRW SKIELERSHV VVCEDIGTLA
ITLKRSGALE QMAFVGIKVK EMSARQGKDF IPSTAQQVQF NPGMTHATWD VLIPDDGIQE
NNEKFRILLD EPVNAVLGRK VKTNVRIINA ENGACPQYLG MISKNHKDVL EVDSFFSPNN
NKKNTDTIIS FNNFNQRGQQ PNPFDNTYNT DPKESSGDSG ANANTRDGLT GKKSSRSSKK
RRRNRKKKKN RKSKSRKTKK INSNDKGSSG NLFNNLSSPS LRIQAPQQCT STTRGLLHFD
DFTQRMYQCD GTSWKAWKAD GSDTKDAPPN GPVPAYQQQC PEGKFFEGKC YVFVTDRKTW
DEAQRACEAI TTMPSVLTPI HSKSHLNFLA KLARKKSFWI GLNNKQTSTQ WVFLRNGNIV
PLVSYTRWGK GQPKSKGSKR NCVLVNKRRK WRNLPCDKPK KRYICEGIPS QNIPSDQPRR
SRGKRKKRID FFGFK
//
