LECH_CHICK
ID LECH_CHICK Reviewed; 207 AA.
AC P02707;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Hepatic lectin;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RX PubMed=7240175; DOI=10.1016/s0021-9258(19)69282-3;
RA Drickamer K.;
RT "Complete amino acid sequence of a membrane receptor for glycoproteins.
RT Sequence of the chicken hepatic lectin.";
RL J. Biol. Chem. 256:5827-5839(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3281941; DOI=10.1016/s0021-9258(18)60740-9;
RA Mellow T.E., Halberg D., Drickamer K.;
RT "Endocytosis of N-acetylglucosamine-containing glycoproteins by rat
RT fibroblasts expressing a single species of chicken liver glycoprotein
RT receptor.";
RL J. Biol. Chem. 263:5468-5473(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2050668; DOI=10.1016/s0021-9258(18)98999-4;
RA Bezouska K., Crichlow G.V., Rose J.M., Taylor M.E., Drickamer K.;
RT "Evolutionary conservation of intron position in a subfamily of genes
RT encoding carbohydrate-recognition domains.";
RL J. Biol. Chem. 266:11604-11609(1991).
CC -!- FUNCTION: Hepatic lectin is a membrane receptor protein that recognizes
CC and binds exposed N-acetylglucosamine moieties of plasma glycoproteins,
CC thus mediating their clearance (from the circulation) and endocytosis.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- PTM: Some or all of the cysteines are involved in disulfide bonds.
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DR EMBL; J03188; AAA48937.1; -; mRNA.
DR EMBL; M63230; AAA48814.1; -; Genomic_DNA.
DR EMBL; M63225; AAA48814.1; JOINED; Genomic_DNA.
DR EMBL; M63226; AAA48814.1; JOINED; Genomic_DNA.
DR EMBL; M63227; AAA48814.1; JOINED; Genomic_DNA.
DR EMBL; M63228; AAA48814.1; JOINED; Genomic_DNA.
DR EMBL; M63229; AAA48814.1; JOINED; Genomic_DNA.
DR PIR; A03167; LNCHL.
DR RefSeq; NP_990815.1; NM_205484.1.
DR AlphaFoldDB; P02707; -.
DR SMR; P02707; -.
DR STRING; 9031.ENSGALP00000042048; -.
DR MEROPS; I63.002; -.
DR iPTMnet; P02707; -.
DR PRIDE; P02707; -.
DR Ensembl; ENSGALT00000070030; ENSGALP00000048786; ENSGALG00000037253.
DR GeneID; 396477; -.
DR KEGG; gga:396477; -.
DR VEuPathDB; HostDB:LOC396477; -.
DR GeneTree; ENSGT00940000164508; -.
DR HOGENOM; CLU_2694088_0_0_1; -.
DR OMA; EWEYFSG; -.
DR OrthoDB; 1118305at2759; -.
DR PhylomeDB; P02707; -.
DR PRO; PR:P02707; -.
DR Proteomes; UP000000539; Chromosome 30.
DR Bgee; ENSGALG00000037253; Expressed in liver and 7 other tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd03590; CLECT_DC-SIGN_like; 1.
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; IPR018378; C-type_lectin_CS.
DR InterPro; IPR033989; CD209-like_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Disulfide bond; Endocytosis;
KW Glycoprotein; Lectin; Membrane; Receptor; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..207
FT /note="Hepatic lectin"
FT /id="PRO_0000046649"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..48
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..207
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 77..203
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:7240175"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7240175"
FT DISULFID 78..92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 109..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 179..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 207 AA; 24216 MW; 1F6B36FDB32899DB CRC64;
MDEERLSDNV RLYKGGSIRQ GLRSFAAVYV LLALSFLLLT LLSSVSLARI AALSSKLSTL
QSEPKHNFSS RDSLLFPCGA QSRQWEYFEG RCYYFSLSRM SWHKAKAECE EMHSHLIIID
SYAKQNFVMF RTRNERFWIG LTDENQEGEW QWVDGTDTRS SFTFWKEGEP NNRGFNEDCA
HVWTSGQWND VYCTYECYYV CEKPLPK
