GenomeNet

Database: UniProt
Entry: T1FR28_HELRO
LinkDB: T1FR28_HELRO
Original site: T1FR28_HELRO 
ID   T1FR28_HELRO            Unreviewed;       546 AA.
AC   T1FR28;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=C-type lectin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=20211275 {ECO:0000313|EnsemblMetazoa:HelroP189456};
GN   ORFNames=HELRODRAFT_189456 {ECO:0000313|EMBL:ESN94635.1};
OS   Helobdella robusta (Californian leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX   NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP189456, ECO:0000313|Proteomes:UP000015101};
RN   [1] {ECO:0000313|Proteomes:UP000015101}
RP   NUCLEOTIDE SEQUENCE.
RA   Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA   Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA   Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA   Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA   Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ESN94635.1, ECO:0000313|Proteomes:UP000015101}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
RN   [3] {ECO:0000313|EnsemblMetazoa:HelroP189456}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
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DR   EMBL; AMQM01001689; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KB097571; ESN94635.1; -; Genomic_DNA.
DR   RefSeq; XP_009027677.1; XM_009029429.1.
DR   AlphaFoldDB; T1FR28; -.
DR   STRING; 6412.T1FR28; -.
DR   EnsemblMetazoa; HelroT189456; HelroP189456; HelroG189456.
DR   GeneID; 20211275; -.
DR   KEGG; hro:HELRODRAFT_189456; -.
DR   CTD; 20211275; -.
DR   HOGENOM; CLU_499019_0_0_1; -.
DR   InParanoid; T1FR28; -.
DR   OrthoDB; 2953303at2759; -.
DR   Proteomes; UP000015101; Unassembled WGS sequence.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR   CDD; cd00037; CLECT; 2.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 3.
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; IPR002889; WSC_carb-bd.
DR   PANTHER; PTHR22801:SF53; 27 KDA PRIMARY MESENCHYME-SPECIFIC SPICULE PROTEIN; 1.
DR   PANTHER; PTHR22801; LITHOSTATHINE; 1.
DR   Pfam; PF00059; Lectin_C; 2.
DR   Pfam; PF01822; WSC; 1.
DR   SMART; SM00034; CLECT; 2.
DR   SMART; SM00321; WSC; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 2.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 3.
DR   PROSITE; PS51212; WSC; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015101};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..546
FT                   /note="C-type lectin domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010980909"
FT   TRANSMEM        452..479
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          40..161
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          106..198
FT                   /note="WSC"
FT                   /evidence="ECO:0000259|PROSITE:PS51212"
FT   DOMAIN          201..247
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          277..396
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   REGION          516..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..537
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   546 AA;  60104 MW;  A5B3F69995076E99 CRC64;
     MFHQIRDIVI FCLFFLSSSR AVFEITDCHK TAKRGDGLVC YKIFKTKNNF ESSVGVCDNN
     NMKLATVGSD DEYAAVMELL RSSRDDDVWI GLKQFQTPWK WSDGSELKEQ GCFLSVSTTN
     HDTRLMATKT GDNSALSCST ICSNNKYNYT GLRNTVECYC GDSFGVETQN GAQCDMPCPG
     SSTENCGGLN SERIVNMNGL YSNWLNGQPN NGSSESPENQ ACATIVKDQN GGWGDVNCMT
     SLRAVCEIGL SSSFPTCDNA TQEEVHKLSY KDASNQDTTT CIYISSRYEN YLNAIQTCNN
     VNGNLIKITS QSHNDALFNV LNNFVKDGST EFWIGLSRIN FRWTTGDILS YTKFTSLSYN
     KKELCAIVRT NPLNDNNEPY IWSLDDCASS KVSLCQSTNA TYIFKPTYFM PTTTTTTLLP
     TKSIVPGQST TLPQVNITVP DASFVAINNN KVMYAAIGGS IGGVVLVVIV TIVIVVVICK
     KKHKMPAMKA DVERTKSVFV EPTYFFGASI ENETTLPSSE TKIEDTSATD PNNQPDLVIS
     SSPPPY
//
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