ID A0A553QDW3_9TELE Unreviewed; 1654 AA.
AC A0A553QDW3;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Lymphocyte antigen 75 {ECO:0008006|Google:ProtNLM};
GN ORFNames=DNTS_031498 {ECO:0000313|EMBL:TRY88118.1};
OS Danionella translucida.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danionella.
OX NCBI_TaxID=623744 {ECO:0000313|EMBL:TRY88118.1, ECO:0000313|Proteomes:UP000316079};
RN [1] {ECO:0000313|Proteomes:UP000316079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bolton {ECO:0000313|Proteomes:UP000316079};
RA Kadobianskyi M., Schulze L., Schuelke M., Judkewitz B.;
RT "Hybrid genome assembly and annotation of Danionella translucida.";
RL bioRxiv 0:0-0(2019).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TRY88118.1}.
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DR EMBL; SRMA01026066; TRY88118.1; -; Genomic_DNA.
DR Proteomes; UP000316079; Unassembled WGS sequence.
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; 9.
DR CDD; cd00062; FN2; 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; 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:SF65; LYMPHOCYTE ANTIGEN 75; 1.
DR PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1.
DR Pfam; PF00040; fn2; 1.
DR Pfam; PF00059; Lectin_C; 8.
DR SMART; SM00034; CLECT; 9.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 10.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 9.
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, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000316079};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1603..1624
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 165..213
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 227..342
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 368..464
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 483..591
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 634..775
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 916..1009
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1032..1137
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1172..1282
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1326..1426
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1467..1593
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 170..196
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 184..211
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 1654 AA; 188878 MW; 40A14974C00358EC CRC64;
MYWHKQQVFF STILILLGGS GVRFGICASP LNSGDDSFTI QHSSIGKCLL VQKGLLKLGD
CSSAPAAQWK WGSAHRLFHM ESSMCLGLEV RSKTVTLFGC DSSEILHWKC YEDVIYTEYQ
MKLSVSSEDS VVAKRDGHDG WKRGGGSENI CQRPYQRMHT SGGNSKGAPC EFPFLYKGTW
HHNCLPGTDD TVLEWCSTTA NYDLEEKWGN CLKYVEGCSA LWEKGPGNGR CYQVVSTALV
TWHEARDACR SQGGDLLSLS SPKELDFFKD RTDLPSKLWM GLNHLDWMQG WQWADGSALA
FAPWETGIPI RSLMSDEDCG VLKEPLHFGA ETCENRLPFI CMKKEKDSGR TDRDIYKPTE
CGEGWTGWKG FCYKLHSAKE SRLSQFEAQR TCEMDKSKLA SLHSFEDIEM LHSNFHSEPV
TFTYWGRAQP PPLLPNTLNC VYYTGEHHTW SVSDCETPRA YMCKQKGKVN ESAAEDGCLV
EGNWKRHGDA CYKVDTELVF YKNSCHISIK NRFEQAFINS LLKEHISTEV QYFWMGLQDS
KGSGEYQWIS QDETIDRAMY TNWKWQEPAS AGGCVVMSTG NPLGQWSVKN CTLFKAGNIC
KKPIKSVVMP IPDPFVPNPN ASCAPGWVSR EGLNYCYKVF HEERVTRKRS WEEAERFCES
LGGHLPSFTE VKDMEVLHYI LRDSISDNRF FWLGLNRRNP NNNNNWEWSD GSAVSMMIFP
EELNEDDDYN RDCVAFKTIK ANYRPLFFPL FHNVPPRSFY PSTFHCDAKL EWVCQIPRGQ
TPKTPEWYNP DGHHNTSVFV DGQEFWFVTE PKLSFEEAVM YCSSNSSKLA APNSFNAARH
LQEHLFEHSG QKIMRLSPMH YYHTAFLGRC PSITPVSFDP GFRTSCNEKQ PFICETLNIT
SLEIGTPEPR PAGSPFKEAS ELCQRLKGSL LSISDQAEQD FITTLLPKLP DEPQKVWIGL
KFKLPDSQWA DGSPQYYEED QLELCAYMYN TDHSDVIGTW DYTSCSDRLN HTICQHLSDK
QEEPQPENNF MVNNHTFQVL QQDNLTWIEA LQLCRNYSMT LTSVPNAYIQ AVLTVQASRR
GKPLWIGLFS EDEGEHFRWT DHSHTEFNRW GSEATEGSCV YLDTDGFWKA TVCEEELSGA
FCHVPHIDTS ITPEVDPVKC PHKSNGQSWI RFKRNCYTLL LTSSRWANVD QISDQQICKT
LAVSGEILTI RDEEENEFIR QQLMPFKNLA MYVWLGMKRN ISDDQPKWLD GTNVQFSNWR
NGDRPNITDP FMVGLSWNGE WEILTKPRLF DTFRQQSIVV CKIENEPKTE FRKSVLEVDA
PDDIRYRRVA KKMDWYQALQ ECGRNGGHLA SITDKDTNEN LALIAKRDGF PLWIGLSKQD
VNRWPFEWSD GTAFKFKPDG FMDDGYDSEE KCVFIDSKGT WSAVNCHVAV QGAICYNHIG
DGNAAHLSSQ SSSACPRSGD QSSWVLFKDH CYAFNAYNYS VYTMEDAKSM CKKLDSSSQL
LSIKSQEEND FVSEYMTQNP SITNRVWLAL NVDSRGKPSG WLDGSDLGFT QWDSKLHWVS
SMQESSQNCA VMISSLGSWT QSSCSESRSR VVCKAPAHPG SPVALIFFIF VLICLLVAVS
FILYQRNKHR FHSTVRYRRN FDDADSTSII NDEE
//
