ID A0A670JHK2_PODMU Unreviewed; 1380 AA.
AC A0A670JHK2;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Mannose receptor C-type 1 {ECO:0008006|Google:ProtNLM};
OS Podarcis muralis (Wall lizard) (Lacerta muralis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Laterata;
OC Lacertibaenia; Lacertidae; Podarcis.
OX NCBI_TaxID=64176 {ECO:0000313|Ensembl:ENSPMRP00000022572.1, ECO:0000313|Proteomes:UP000472272};
RN [1] {ECO:0000313|Ensembl:ENSPMRP00000022572.1, ECO:0000313|Proteomes:UP000472272}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30819892; DOI=10.1073/pnas.1820320116;
RA Andrade P., Pinho C., Perez I de Lanuza G., Afonso S., Brejcha J.,
RA Rubin C.J., Wallerman O., Pereira P., Sabatino S.J., Bellati A.,
RA Pellitteri-Rosa D., Bosakova Z., Bunikis I., Carretero M.A., Feiner N.,
RA Marsik P., Pauperio F., Salvi D., Soler L., While G.M., Uller T., Font E.,
RA Andersson L., Carneiro M.;
RT "Regulatory changes in pterin and carotenoid genes underlie balanced color
RT polymorphisms in the wall lizard.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:5633-5642(2019).
RN [2] {ECO:0000313|Ensembl:ENSPMRP00000022572.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR Ensembl; ENSPMRT00000023987.1; ENSPMRP00000022572.1; ENSPMRG00000014572.1.
DR GeneTree; ENSGT01050000244842; -.
DR OMA; AQEFCRM; -.
DR Proteomes; UP000472272; Chromosome 12.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00037; CLECT; 8.
DR CDD; cd00062; FN2; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 8.
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; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR22803:SF155; C-TYPE LECTIN DOMAIN CONTAINING 10A; 1.
DR PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1.
DR Pfam; PF00040; fn2; 1.
DR Pfam; PF00059; Lectin_C; 8.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR PRINTS; PR00013; FNTYPEII.
DR PRINTS; PR01504; PNCREATITSAP.
DR SMART; SM00034; CLECT; 8.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 8.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 4.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 8.
DR PROSITE; PS51092; FN2_2; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00479}; Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000472272};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 191..239
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 249..364
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 399..516
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 534..649
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 678..781
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 784..909
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 937..1061
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1083..1194
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1219..1333
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 196..222
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 210..237
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 1380 AA; 157731 MW; 90679377E79B6E70 CRC64;
MNVESYCPRI NKTEQWIVKI NYRINTRGIS LSRLSMLLLH IMNPGIILSS DSFLIYNENL
KLCIQAQKSH SPILDYCDKD NEGQHFKWIS NDQILNMAVK LCLAVPSKSD QARVMLSPCN
ETTELQKWEC RNDNLLVLDQ EDLFLNPEGG QKSRLMLSKV ATSKSTWKIS GTKENWCSKH
YEALYTLRGN AQGAPCVFPF KYQDKLYAQC IRDGDEHGQL WCGTTADVDR DSLTGYCPIK
GKHLAINHWT GDFYQVNSDS ALTWYQARKS CQQQNAELLS ITDLQEQVYV TGLTSCMPTD
LWIGLNSLDD ESGWQWMGNY PLRYLNWAPG SPTPETERIC GSMLSKVGKW ENNKCQEKLG
YICKKANSSL DASVIPSENE GDLPGSHLLR SCPDGWVAYA GHCYHLSRDP KTWKSALSSC
RKEGGDLISI HHIEEYSFVI SQLGYQPTDL LWIGLNDQKT QMYYEWSDGT KVTFTKWQKG
KPTQINDVQN ECVIMNGEGG YWADYFCEVE LGYICKRKPS GVLPEEPEIG WKRHGNYCYL
IGQTSLTFSE AKMFCETNKG SLTSVENRYE QAYLTSLVGL HSEKYLWIGL SDVQQPGTFI
WTRGDSALFT HWNSEMPGQH SGCVAMRTGT AAGLWDVVNC EEKATFICKQ WVEGVTTTPA
PKPTPLQPCP VGWRPSSTRN VCFKAYTKNK SNKKSWFEAR EFCRAVGGEL ISIHSEEEQK
ILEEMRSNDN YWIGLNNVDP DKGFTWSDGS NVRYLRTTLN KINKNMSSFA DYSFKIIDNG
WILYEEHEYY VSNTSTSAER ARALCKKHGG DLTVIESETE RKFLWKYVRN IWNICFPNEF
FFIGKLHSSV PFSLTIFYSW LDQTPVTYVS WAPGEPDSGN DDETCVAMKA ITGLWYDTNC
GTANKFICER HNSSVRSTVA PTMPVPVGGC ADGWLFFNNK CFQLFGFNEE DRKNWSDART
ACKKQGGNLA SITSKAFQAF LTVHLKSAST DAWIGLNDIH SEHTFLWTDG SGVHYLNWAK
GFPRFWSVST ENCVFMMKEP EKLAGNWKDG PCSAKKSYIC QRNSDPALSH PETTISASGY
TVFGNSSYSL IGPKMTWEAA RKKCHSIQSE LASIVNPYIQ SFLLLHVLKY KEPVWIGLNS
NMTGERYKWI SNQRLVYTDW GPEEPKQKIA CVYLHPDGHW KTGNCNETFF TVCKIPTEPP
EAPGKCPESK QNQISWIPFR AHCYKFFTGW FDRPEAHFKC SQLEDLAELK FLVEHTQQNT
RWNYWIGLIR NIEGEWLWED KTEVDFVNWK ANEPTFEPED YSSYYSGICA YMKADNGEWY
KEHCRRSNGF ICKRHKSKTF SYLLFIRVIS LSALLLKLCN KGVSVRLLPR EGLFPISACL
//
