ALPS_PORTR
ID ALPS_PORTR Reviewed; 123 AA.
AC C0KJQ4; C6K7B2; E7CRH9; E7CRI0; E7CRI7; E7CRJ1; E7CRJ8; E7CRK1; E7CRK2;
AC E7CRK4; E7CRK5; E7CRK6; E7CUG9; E7CUH0;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=Anti-lipopolysaccharide factor {ECO:0000303|PubMed:20167286, ECO:0000303|PubMed:21168510, ECO:0000312|EMBL:ACM89169.2};
DE Short=PtALF {ECO:0000303|PubMed:20167286};
DE Flags: Precursor;
GN Name=ALF {ECO:0000312|EMBL:ACS45385.2};
OS Portunus trituberculatus (Swimming crab) (Neptunus trituberculatus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC Eubrachyura; Portunoidea; Portunidae; Portunus.
OX NCBI_TaxID=210409;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ACM89169.2}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Hemocyte {ECO:0000269|PubMed:20167286};
RX PubMed=20167286; DOI=10.1016/j.cbpb.2010.02.003;
RA Yue F., Pan L., Miao J., Zhang L., Li J.;
RT "Molecular cloning, characterization and mRNA expression of two
RT antibacterial peptides: crustin and anti-lipopolysaccharide factor in
RT swimming crab Portunus trituberculatus.";
RL Comp. Biochem. Physiol. 156:77-85(2010).
RN [2] {ECO:0000305, ECO:0000312|EMBL:ACS45385.2}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE
RP SPLICING, TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Eyestalk {ECO:0000269|PubMed:21168510};
RX PubMed=21168510; DOI=10.1016/j.fsi.2010.12.005;
RA Liu Y., Cui Z., Luan W., Song C., Nie Q., Wang S., Li Q.;
RT "Three isoforms of anti-lipopolysaccharide factor identified from eyestalk
RT cDNA library of swimming crab Portunus trituberculatus.";
RL Fish Shellfish Immunol. 30:583-591(2011).
CC -!- FUNCTION: May bind to bacterial LPS and thus specifically inhibit the
CC LPS-mediated activation of the hemolymph coagulation. It has a strong
CC antibacterial effect especially on the growth of Gram-negative bacteria
CC (By similarity). {ECO:0000250|UniProtKB:B5TTX7}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:21168510}; Synonyms=PtesALF3
CC {ECO:0000303|PubMed:21168510};
CC IsoId=C0KJQ4-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:21168510}; Synonyms=PtesALF1
CC {ECO:0000303|PubMed:21168510};
CC IsoId=C0KJQ4-2; Sequence=VSP_041458;
CC -!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in muscle and
CC stomach, moderately in heart and gill and at lower levels in hemocytes
CC and hepatopancreas. Isoform 2 is mainly expressed in gill,
CC hepatopancreas, muscle and eyestalk. {ECO:0000269|PubMed:20167286,
CC ECO:0000269|PubMed:21168510}.
CC -!- INDUCTION: By injection with live V.alginolyticus. Isoform 2 expression
CC is highest 24 hours post-injection. Expression of isoform 1 and isoform
CC 2 is reduced at 3 hours post-injection, increases to a peak at 12 hours
CC post-injection, and returns to control levels at 32 hours post-
CC injection (PubMed:21168510). Isoform 1 expression is up-regulated at 3
CC and 24 hours post-injection and reaches a peak at 48 hours post-
CC injection (PubMed:20167286). {ECO:0000269|PubMed:20167286,
CC ECO:0000269|PubMed:21168510}.
CC -!- MISCELLANEOUS: [Isoform 1]: Major isoform.
CC {ECO:0000269|PubMed:21168510}.
CC -!- MISCELLANEOUS: [Isoform 2]: Minor isoform detected in approximately 30%
CC of the cDNA clones. May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000269|PubMed:21168510}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ADU25043.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; FJ612108; ACM89169.2; -; mRNA.
DR EMBL; GQ165621; ACS45385.2; -; mRNA.
DR EMBL; HM536671; ADU25060.1; -; Genomic_DNA.
DR EMBL; HM536672; ADU25061.1; -; Genomic_DNA.
DR EMBL; HM536673; ADU25062.1; -; Genomic_DNA.
DR EMBL; HM536674; ADU25063.1; -; Genomic_DNA.
DR EMBL; HM536675; ADU25064.1; -; Genomic_DNA.
DR EMBL; HM536676; ADU25065.1; -; Genomic_DNA.
DR EMBL; HM536677; ADU25066.1; -; Genomic_DNA.
DR EMBL; HM536678; ADU25067.1; -; Genomic_DNA.
DR EMBL; HM536679; ADU25068.1; -; Genomic_DNA.
DR EMBL; HM536680; ADU25069.1; -; Genomic_DNA.
DR EMBL; HM536681; ADU25070.1; -; Genomic_DNA.
DR EMBL; HM536682; ADU25071.1; -; Genomic_DNA.
DR EMBL; HM536683; ADU25072.1; -; Genomic_DNA.
DR EMBL; HM536684; ADU25073.1; -; Genomic_DNA.
DR EMBL; HM536685; ADU25074.1; -; Genomic_DNA.
DR EMBL; HM536686; ADU25075.1; -; Genomic_DNA.
DR EMBL; HM536687; ADU25076.1; -; Genomic_DNA.
DR EMBL; HM536688; ADU25077.1; -; Genomic_DNA.
DR EMBL; HM536689; ADU25078.1; -; Genomic_DNA.
DR EMBL; HM536690; ADU25079.1; -; Genomic_DNA.
DR EMBL; HM536691; ADU25080.1; -; Genomic_DNA.
DR EMBL; HM536692; ADU25081.1; -; Genomic_DNA.
DR EMBL; HM536693; ADU25082.1; -; Genomic_DNA.
DR EMBL; HM536694; ADU25083.1; -; Genomic_DNA.
DR EMBL; HM536695; ADU25084.1; -; Genomic_DNA.
DR EMBL; HM536696; ADU25085.1; -; Genomic_DNA.
DR EMBL; HM536697; ADU25086.1; -; Genomic_DNA.
DR EMBL; HM536698; ADU25087.1; -; Genomic_DNA.
DR EMBL; HM536699; ADU25088.1; -; Genomic_DNA.
DR EMBL; HM536700; ADU25089.1; -; Genomic_DNA.
DR EMBL; HM627757; ADU25042.1; -; mRNA.
DR EMBL; HM627758; ADU25043.1; ALT_FRAME; mRNA.
DR AlphaFoldDB; C0KJQ4; -.
DR SMR; C0KJQ4; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR Gene3D; 3.30.160.320; -; 1.
DR InterPro; IPR024509; Anti-LPS_factor/Scygonadin.
DR InterPro; IPR038539; Anti-LPS_factor/Scygonadin_sf.
DR Pfam; PF11630; DUF3254; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Antibiotic; Antimicrobial; Disulfide bond;
KW Glycoprotein; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..123
FT /note="Anti-lipopolysaccharide factor"
FT /evidence="ECO:0000255"
FT /id="PRO_0000410488"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..76
FT /evidence="ECO:0000250|UniProtKB:P07086"
FT VAR_SEQ 86..123
FT /note="SRTKSRSGSSREATKDFVRKALQNGLVTQQDASLWLNN -> CKYCVVF
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:21168510"
FT /id="VSP_041458"
FT CONFLICT 44..45
FT /note="HN -> RS (in Ref. 2; ADU25082)"
FT /evidence="ECO:0000269|PubMed:21168510"
FT CONFLICT 47
FT /note="S -> P (in Ref. 2; ADU25086)"
FT /evidence="ECO:0000269|PubMed:21168510"
FT CONFLICT 50
FT /note="F -> L (in Ref. 2; ADU25082)"
FT /evidence="ECO:0000269|PubMed:21168510"
FT CONFLICT 55
FT /note="C -> Y (in Ref. 2; ADU25085)"
FT /evidence="ECO:0000269|PubMed:21168510"
FT CONFLICT 66
FT /note="F -> S (in Ref. 2; ADU25086)"
FT /evidence="ECO:0000269|PubMed:21168510"
FT CONFLICT 73
FT /note="K -> R (in Ref. 2; ADU25083)"
FT /evidence="ECO:0000269|PubMed:21168510"
FT CONFLICT 74
FT /note="F -> L (in Ref. 2; ADU25086)"
FT /evidence="ECO:0000269|PubMed:21168510"
FT CONFLICT 76
FT /note="C -> R (in Ref. 2; ADU25079)"
FT /evidence="ECO:0000269|PubMed:21168510"
FT CONFLICT 79
FT /note="W -> R (in Ref. 2; ADU25079)"
FT /evidence="ECO:0000269|PubMed:21168510"
FT CONFLICT 100
FT /note="K -> E (in Ref. 2; ADU25087)"
FT /evidence="ECO:0000269|PubMed:21168510"
FT CONFLICT 103
FT /note="V -> A (in Ref. 2; ADU25072)"
FT /evidence="ECO:0000269|PubMed:21168510"
FT CONFLICT 115
FT /note="Q -> L (in Ref. 2; ADU25068)"
FT /evidence="ECO:0000269|PubMed:21168510"
FT CONFLICT 120..123
FT /note="Missing (in Ref. 2; ADU25061)"
FT /evidence="ECO:0000269|PubMed:21168510"
FT CONFLICT 121
FT /note="L -> R (in Ref. 2; ADU25087)"
FT /evidence="ECO:0000269|PubMed:21168510"
SQ SEQUENCE 123 AA; 14109 MW; B8389D0A9CC4BBFC CRC64;
MRKGVVAGLC LALVVMCLYL PQPCEAQYEA LVTSILGKLT GLWHNDSVDF MGHICYFRRR
PKIRRFKLYH EGKFWCPGWA PFEGRSRTKS RSGSSREATK DFVRKALQNG LVTQQDASLW
LNN
