ID   LADD_ONCMY              Reviewed;         190 AA.
AC   P81018;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   29-OCT-2014, sequence version 2.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Ladderlectin;
DE   Flags: Precursor;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX   PubMed=18407519; DOI=10.1016/j.fsi.2007.11.002;
RA   Russell S., Young K.M., Smith M., Hayes M.A., Lumsden J.S.;
RT   "Cloning, binding properties, and tissue localization of rainbow trout
RT   (Oncorhynchus mykiss) ladderlectin.";
RL   Fish Shellfish Immunol. 24:669-683(2008).
RN   [2]
RP   PROTEIN SEQUENCE OF 45-55.
RC   TISSUE=Blood;
RX   PubMed=9149391; DOI=10.1016/s0305-0491(96)00273-8;
RA   Jensen L.E., Thiel S., Petersen T.E., Jensenuis J.C.;
RT   "A rainbow trout lectin with multimeric structure.";
RL   Comp. Biochem. Physiol. 116B:385-390(1997).
CC   -!- FUNCTION: Lectin that binds sepharose in a calcium-dependent manner.
CC   -!- SUBUNIT: Multimeric.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1 {ECO:0000305}; Synonyms=RTLL-2 {ECO:0000303|PubMed:18407519};
CC         IsoId=P81018-1; Sequence=Displayed;
CC       Name=2 {ECO:0000305}; Synonyms=RTLL-1 {ECO:0000303|PubMed:18407519};
CC         IsoId=P81018-2; Sequence=VSP_057102;
CC   -!- TISSUE SPECIFICITY: Expressed in cells of the branchial epithelium,
CC       hepatic sinusoids, biliary epithelium, renal interstitium, skin, and
CC       sub-mucosal granular layer of the intestine. Highly expressed in caudal
CC       kidney. Moderately expressed in liver. Weakly expressed in gill,
CC       spleen, cranial kidney and skin. Isoform 1 is highly expressed in
CC       intestine. Isoform 2 is weakly expressed in intestine.
CC       {ECO:0000269|PubMed:18407519}.
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DR   AlphaFoldDB; P81018; -.
DR   SMR; P81018; -.
DR   GO; GO:0005903; C:brush border; IDA:AgBase.
DR   GO; GO:0044194; C:cytolytic granule; IDA:AgBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR   GO; GO:0005829; C:cytosol; IDA:AgBase.
DR   GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0008061; F:chitin binding; IDA:AgBase.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Direct protein sequencing; Disulfide bond;
KW   Lectin; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..190
FT                   /note="Ladderlectin"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000084351"
FT   DOMAIN          60..179
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        153..169
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   VAR_SEQ         21..34
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:18407519"
FT                   /id="VSP_057102"
FT   CONFLICT        10
FT                   /note="L -> M (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        54
FT                   /note="T -> P (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        101..105
FT                   /note="EVVAS -> AIAGC (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113
FT                   /note="P -> T (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        159
FT                   /note="R -> G (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        167
FT                   /note="I -> M (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   190 AA;  21306 MW;  F5D2555CF6D70844 CRC64;
     MAMLTISLLL CAAVALNGAT VLELFQDFEQ ALHLGAKGED ERVVAAENRN QCPTGWFQFG
     SRCFMFVETA RSWPLAERHC VSLGANLASV HSSAEYQFLQ EVVASKTGGF STPWIGGFDA
     VQDRLWFWSD GSEFDYQNWK KGEPNNSGGR EPCIVINWRD EYRWNDINCG NSFPSGVLQK
     NVEIQKNEPT