ID A0A3P8PQ79_ASTCA Unreviewed; 1316 AA.
AC A0A3P8PQ79;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Mannose receptor, C type 1b {ECO:0000313|Ensembl:ENSACLP00000019153.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000019153.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000019153.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000019153.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00479}.
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DR STRING; 8154.ENSACLP00000019153; -.
DR Ensembl; ENSACLT00000019596.1; ENSACLP00000019153.1; ENSACLG00000013001.1.
DR GeneTree; ENSGT01050000244842; -.
DR OMA; WIGLHYL; -.
DR Proteomes; UP000265100; Chromosome 18.
DR Bgee; ENSACLG00000013001; Expressed in spleen.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 9.
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; IPR013806; Kringle-like.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR22803:SF124; C-TYPE LECTIN DOMAIN FAMILY 19 MEMBER A-RELATED; 1.
DR PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1.
DR Pfam; PF00040; fn2; 1.
DR Pfam; PF00059; Lectin_C; 6.
DR SMART; SM00034; CLECT; 8.
DR SMART; SM00059; FN2; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 8.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 2.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 7.
DR PROSITE; PS00023; FN2_1; 1.
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1316
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018153395"
FT DOMAIN 150..197
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 208..318
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 341..457
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 482..597
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 626..731
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 755..869
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1051..1162
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1197..1293
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 155..181
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 1316 AA; 149373 MW; D583C2EA8EF95C8A CRC64;
FFYKVSYLFF FFCSITTNAI TTNSPFQLTN RGTGFCLIKT NNHCNDIRWT TGDRLLVLQR
NKCLGVQGKS VGSEVNLYDC DEASELQKWE CKNETVLALK GQELYIELTA DNTAILSRTT
GPNNHLTISG TSSGACTRTY RELFTIGGNA AGRPCMFPFL YKTQWYSDCT KFDSSEKRLW
CAVETNYQSE RWGYCPTMSK EDWNMHPTTG AYYQLNIQSA LTWHQAQVSC KQQGASLLSI
DDPHEQAYIT GGNTLWIGLI LDPEHGWKWI NGRPYRYMKW DSGHPLPNPG YNCAVVDPSV
RYLWQSLPCS NKLGYICYSK EAEEAPTRAG TGFCSNPWIH YNGHCFHRNQ AQKTWSEAQV
ACHQDGGDLV SIHSVEDQSF IISQLGYTST DQLWIGMNDR KTEGLFDWSD HSTVTFTSWE
FGKPAVSSEI KDCVLMRGEN GNWADLVCEE QHGFICKKMS ALRPSGEEVE QNTGCKNGWR
RHGSYCYFIG IQTKTFDEAK NDCKGSLSYL ADVSNGVDNA FLVSLVGMRP EKHFWLGLSN
QKNTEEFVWT NTDSVRFTHW NAEMPGNRQG CVAMKTGIFA GLWDVVPCTN KEKYICKHLA
EGAVLTPPPP TLFPPECASG WTRLGFSNRC FKLFDRYSIQ KKTWFEAKDY CRAIGGDLLS
IHSSVELQSV PRYSIKENRT SSWIGLSAPD PDTGYVWSDG TPVSCSFLCI IQKIQSWSDI
HCEKYSEWLC QIRMTPNPFD LFPGYNKTSD GWFEWNRNQY YINRNQMGME DARRYCQQRH
SDLVTISSEA ERVFLWKLVN TGHHPYWIGL IVDLDGTFAW MDDSPVVFQA WSENQPNFQN
NDENCVAITP SRGFWHDYNC GFQLSFICKR NSSMPEHISV VPTVLPKGGC PQDWKKFNSK
VRTWEGARTQ CKNKGGNLAS ILSKHVQGLS FLYYTFSFIT KESKSLNPFI ICVFMLCHTN
RKMYFMLPGK ICSGHMKASK TDPDITLVSL FLFCLSHQRG CAVMTTDRTT GIGKWDQRSC
SDKNGYICLR NLDPSLPDSP EPTANNGYVK ILNDSIKVVT QKMNWDSAKK YCELDGANLA
SLRNEWSQVY VELMALEMEG PLWIGLNKKQ TGYFRPIDGW EMTFSNWDRF EPEMQQSCVY
VNNENGKWKT ADCAHNMASV CMKSTDVPPT ESTESVSFPG NCPEDPASRT GYTWIPFKGY
CYLFVKGSFD WGDASALCIR YGGTLTSIEN PAEAKEKFCL FLGLWKWLDK TAIDFINWGP
NEPGGFGTYG AIASLDGSWT TGRVYSSKGF ICKAPKGKSR NLKNGFVIAQ MCNTYT
//
