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Database: UniProt
Entry: A0A672YPX8_9TELE
LinkDB: A0A672YPX8_9TELE
Original site: A0A672YPX8_9TELE 
ID   A0A672YPX8_9TELE        Unreviewed;      1725 AA.
AC   A0A672YPX8;
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:ENSSORP00005006644.1};
GN   Name=LOC115438801 {ECO:0000313|Ensembl:ENSSORP00005006644.1};
OS   Sphaeramia orbicularis (orbiculate cardinalfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Kurtiformes; Apogonoidei; Apogonidae; Apogoninae; Sphaeramia.
OX   NCBI_TaxID=375764 {ECO:0000313|Ensembl:ENSSORP00005006644.1, ECO:0000313|Proteomes:UP000472271};
RN   [1] {ECO:0000313|Ensembl:ENSSORP00005006644.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   Ensembl; ENSSORT00005006904.1; ENSSORP00005006644.1; ENSSORG00005001995.1.
DR   Proteomes; UP000472271; Unplaced.
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   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; 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   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; 9.
DR   SMART; SM00034; CLECT; 10.
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:UP000472271};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..1725
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5025513212"
FT   TRANSMEM        1674..1695
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          166..214
FT                   /note="Fibronectin type-II"
FT                   /evidence="ECO:0000259|PROSITE:PS51092"
FT   DOMAIN          227..345
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          373..495
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          515..622
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          660..742
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          947..1070
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1098..1202
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1237..1345
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1385..1494
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1538..1663
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   REGION          634..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        636..650
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        171..197
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT   DISULFID        185..212
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ   SEQUENCE   1725 AA;  195832 MW;  368086A1F7F7E5BA CRC64;
     MLKMSKATLC LCLLIVWETT VFLGTCSTAA TSFDEDAFTI QHSDTKKCLG TGDSADLILS
     TCTLNSKSQL WKWGSGHRLF HVATTQCLAL NLRTKALSLV DCGSNMLLWW RCLNEAVYTV
     YQMGLVVSNG KVTVKRDSEE AWVRGGSQDN ICQRPYRVIH TTNGNSAGAP CDFPFKYNDT
     WYHGCLPHVE NPGLSWCSTT PDYDKDRKNG DCLIYEEGCQ TLFEGPEGKT CYEFVPFAAV
     TWQEALDSCR SQGADLLSVS GPEDLHSETF LDGLGRMPER MWIGLHQLDT SQGWQWSDGS
     PFFFLRWEED MPSTSMITES DCGVLNMNQN YESESCNQRL PYICKKTVNA SHTPSEESLV
     YKETLCEVGW VPWNGWCYKM VKDKSLNFMD ALMHCNSTEM GGGFLASFHS IDSKEMISNN
     FHEDGQFLDV WIGLIGSGTS PTVFKWINEA PVTFTYWEPD QPVQLKLDTS CVFYSGESHG
     WRVGDCSKSL PFMCQKKGEV QESAAVAGCL YEDGWRRHGN SCYQVKTKQV FFKDHCNMTI
     RNRFEQAFIS RVLSEHITIE TQYFWIGLQD IKNTGEYQWM SQNRSDGVVT YTNWGWFQPE
     RDGGCAVMST AKPLGKWEVK NCTLFKAGTI CRKDLSPPPS PEPEPDPSAP CPDGWVSRQN
     ISYCYKVFHE ERLSRKRSWK EAEGFCRALG ATLPSFQHFA EMRALHSILR DSISDNRYFW
     IGLNRRNPAD RSWQWSDGQP VSATFCFVTM RSSLKHLFVF LLHDFNPTPF FSTPFHCDAR
     LEWVCQIPRG KTPKTPEWYN PGGHHETSIF VDGGEYWFVK EPKLTFEEAK LYCSTNGSKL
     AVPPSFTAAR QIHQYLPNVS GTSKQKWWVD MKEPGQLFPL TYTQMYLYHS VFLGRCTTIS
     PDNIFPGEYC RQRLPFVCQK HNVTSVEINP MEPHAGGLPC GNDSLAFRNK CYTLMKGTTR
     MPFRTANEEC QSVRGTLVSI SDQVEQDFIT SLLPSMTDMT RVWIGLKLKP NEPKWVDQSP
     VSFLNFNPLL HGMLKPIIIS HLDPESMDLC VFMINNPHSA MMGSWDFASC GESQNLAVCQ
     HYADKLEEPH VPSQPFSVNN HTILLLLKNL TWFEALEQCR QNNMDLASVA DTILQSNLTV
     HVNRARTPMW IGLFSEDDGI HYRWTDHSHT VFSRWSSDVS GGSCVYLDTD GFWKTTECEE
     ELGGAICHKP HNEIITTPED VAVKCPHKIN GPNWIPFKNN CYSFQLVASR WEQFDQGQIH
     ETCTKLHASA DILTVRNEEE NEFIRQQLMP FRNLVQFIWL GMFKDDNDNQ MKWYDGTNVQ
     YSKWKFGRPD INKPFLAGLN AQGLWFLLTN KLYFSDFKQK TIVACKLDRE PKQNYNQSVA
     DFQYYGNLTY QVVTRRLSWY QAVEECGRRG GHLASVHDIQ HSAHVELIAK TDGFALWIGL
     SSQDASGADY EWSDGTKFNY KPTISEAKES SSSESQEAGC VFVTPAGVWV RTSCHTMVEG
     AICYTTNITT ASQRAKHQAI PVANRCPQID GMSKWVQHQD HCYAFDTSFY NYSIYSMEQA
     KSVCQNMDAE LLMIKTKEEN DFVSQYTLDD PHVTSRVWLG MNLDSQDKPV AWLDGSGVGF
     SNWKSGALAS GKASEPRCAV MTAGEGGMWS LVSCRNSLSR VVCKTKAKST GSPVALGFFI
     VLLIALLLAV AFIVYKKKRA SFSSTVRYKR TFDETDTTSI ITEAE
//
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