ID A0A667YF76_9TELE Unreviewed; 1615 AA.
AC A0A667YF76;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Lymphocyte antigen 75-like {ECO:0000313|Ensembl:ENSMMDP00005019906.1};
GN Name=LY75 {ECO:0000313|Ensembl:ENSMMDP00005019906.1};
OS Myripristis murdjan (pinecone soldierfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Holocentriformes; Holocentridae; Myripristis.
OX NCBI_TaxID=586833 {ECO:0000313|Ensembl:ENSMMDP00005019906.1, ECO:0000313|Proteomes:UP000472263};
RN [1] {ECO:0000313|Ensembl:ENSMMDP00005019906.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR Ensembl; ENSMMDT00005020378.1; ENSMMDP00005019906.1; ENSMMDG00005009461.1.
DR GeneTree; ENSGT01050000244842; -.
DR Proteomes; UP000472263; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00037; CLECT; 10.
DR CDD; cd00062; FN2; 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; 10.
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 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; 9.
DR PRINTS; PR01504; PNCREATITSAP.
DR SMART; SM00034; CLECT; 10.
DR SMART; SM00059; FN2; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 10.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 9.
DR PROSITE; PS51092; FN2_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00479};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000472263};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1564..1585
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..102
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 115..233
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 261..384
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 404..511
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 552..691
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 841..966
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 991..1095
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1130..1239
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1278..1384
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1428..1553
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 523..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 59..85
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 73..100
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 1615 AA; 183076 MW; 55EBA16A719B40D9 CRC64;
MEGVVYTVYQ MGLSVNNGKV GAKRDSVDAW TRDASQDNIC QRPYRVVHTT HGNSAGAPCD
FPFLYNGSWH HGCLPAEDYP GMSWCATTSD YDQDKKMGHC LIPEEGCQTL FAGQEGGTCY
EFVPGAAVTW YEALDSCRSQ EADLLSLSGP EELFSTSLMG GLGKMPDKMW IGLHQLDTSQ
GWQWSDDSPL SYLRWESGSP DTSILVESDC GVLNSKKNYE SESCNKRLPY VCKKRVNASH
TTTTESTAYK ETVCADGWVP WSGWCYRLVK DEPQNFVDAQ LHCNNTEGGG GGSLASFHSL
DSKEMMSTNF QQEGQVLDVW IGLIGTGMDS IVFKWADEMP VTFTYWGPNE PSQPAQDPGC
VFYSGPSHGW RVGNCTEKLP FMCQKKGEVR ESATELGCPP EGGWKRHGNS CYQVNTKKVS
FKDRCNIAIR NRFEQAFISR LLVEQISRET QYFWIGLQDI KNTGEYQWLS QNGSQDPVMY
TNWGSSEPDR DGGCAVMSTA KPLGKWEVKN CTIFKAGTIC KTDLTPPPAP EPEPSSNTSC
PQGWMSRTGV KYCYKVFHKE RLSRTRSWEE AERFCQALGA NLPSFTRQEE MTALHYVMRD
TISDSRFFWV GLNRRNPADR SWEWSDGRPV PMGVLHHDLH EDDAYNRNCA AFKTMRNSLK
HLFEFLLHDI RPRPFYATPF HCDARLEWVC QIPRGKKPKT PDWYNPGGHH ETSIFVDDRE
FWFVSEPKLT FEEARLFCSA NGSQLAVPHS FTAATQIHQY LAKVSSSPQQ SWWADVREPG
RFYPMTHAHM LAVICLVTEY DNSCERRLPF VCERHNTTSV ERDPLEPHAG GLACENGSIA
FRNKCYTVVK PFRHWTFMQA NEECKSLKGT LVTISDQVEQ DFITTLLPEM EKIEKIWIGL
KLKTEDPQWM DESPVSFVNF NPLLHGMLRP IRVNLLTDNM ELCVFMITNN NSAMMGTWDY
TTCSEQQHLG ICQHYADKPE EPKFPSELLH INNHSILLLQ GNLTWPEALK QCKDNNMDLA
SVSDTFLQSV LTVHVSRART PMWIGLFSTD EGIHYHWSDN SHIVFSRWSS EGTSGSCVYL
DTDGFWKATE CEEELGGAIC HEPHKETITT PEDAIVKCPH KINGPTWFPF KNNCYSFQLV
SSRWDQFNRG LIRDTCKDLD EKAEILTIRN AEENEFVKQN LIPFRNLVQF VWLALFKDDN
DNQMKWYDDT NVQYSNWRNG RPDIEGDFMA GLNPDGVWEL ITYRPYFADF KQRSIVACKL
DNESKEQYSQ TLKDFQNYGS LTYQVVKRKL SWFQALEECG RRGGHLASVH DIQHDAHLGH
IARTDGFPLW IGLSNQDASS SAYEWSDGTG YEYSAISQEG SSSVDQQTGC VFITHTGSWV
RADCHTLVEG AICYNTTKTT LSQRAKLQAA PVTKNCPQSS GAASWVQYQD HCYAFDMSFF
NYSVYNMEKA KNICQNLDAH LLTINTKEEN EFVTKYMSDN PLITSRVWLG MDLDTQGKPV
AWLDGSALAF SNWKNGEAVS KVSSEAPCAV MVSADKGVWN HVSCKDNHSR VVCKVAARSG
GSPVALGFFL VVVIALLSAI GFIIYKKKRA YFSSTVRYKR NFDEADTTSI ITEAD
//
