ID A0A2R2MJK4_LINUN Unreviewed; 1048 AA.
AC A0A2R2MJK4;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Uncharacterized protein LOC106180720 {ECO:0000313|RefSeq:XP_023930406.1};
GN Name=LOC106180720 {ECO:0000313|RefSeq:XP_023930406.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_023930406.1};
RN [1] {ECO:0000313|RefSeq:XP_023930406.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26383154;
RA Luo Y.J., Takeuchi T., Koyanagi R., Yamada L., Kanda M., Khalturina M.,
RA Fujie M., Yamasaki S.I., Endo K., Satoh N.;
RT "The Lingula genome provides insights into brachiopod evolution and the
RT origin of phosphate biomineralization.";
RL Nat. Commun. 6:8301-8301(2015).
RN [2] {ECO:0000313|RefSeq:XP_023930406.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00122}.
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DR RefSeq; XP_013420249.1; XM_013564795.1.
DR RefSeq; XP_023930406.1; XM_024074638.1.
DR AlphaFoldDB; A0A2R2MJK4; -.
DR EnsemblMetazoa; XM_024074638.1; XP_023930406.1; LOC106180720.
DR KEGG; lak:106180720; -.
DR InParanoid; A0A2R2MJK4; -.
DR OrthoDB; 2879388at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR CDD; cd00037; CLECT; 1.
DR CDD; cd01099; PAN_AP_HGF; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.120.740; -; 1.
DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 2.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR036262; Resistin-like_sf.
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; PF02140; Gal_Lectin; 1.
DR Pfam; PF13385; Laminin_G_3; 2.
DR Pfam; PF00059; Lectin_C; 2.
DR SMART; SM00034; CLECT; 2.
DR SMART; SM00473; PAN_AP; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57414; Hairpin loop containing domain-like; 1.
DR SUPFAM; SSF111423; Resistin; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS50228; SUEL_LECTIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1048
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015106197"
FT DOMAIN 214..381
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 388..501
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 511..596
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 611..700
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 699..787
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
SQ SEQUENCE 1048 AA; 117298 MW; D877C8AA129E5398 CRC64;
MESSYVGRIF PFVLMMLVFA AHIEAKHFSA LQPITYFDGS TDIDHADASL ATFGGTDHTV
IAWFKTYASN GGIFAKTASG TTWASKGKCF YIRDGNIQTD SHGIGYIRGS KVVNDGKWHM
AAWQFTASSN SYRLTVDGVQ DTTGTLALAT DDGNHVMRIG NCADNFVGKF TGHLHTVMYY
DYRIGNTDLE YVYRNSLNSR EYIWIEETYF GGDGQYYKNS TEAWTAVPNW SRKFNNFGKF
DFSLSVWVRT THTGSILRRT ESSGTWVSHG KVLYINSAGK AMFDAYSVGN VVSTSIVSDD
QWHFIVFTQE MQTTATWRIY VDGVLEASQQ SMAMTEDLGD HVIFIANTFQ GYLKELFYYN
YKISDEEILS RYNGFQDDTH CPTGWHPFQG SCYYFEEANS IGYDGIQAKD FCHSLGAKRA
SISSQLEQDF LYHVLQKMNY TGRDWWLGLQ QEDSSVNEYN FWDDGSRVLW SLWDSRDPDS
SAKDCVRCLQ DRAMEWNDRW CVYGDLWNVV CEKPEECRFV HIEGQKINLN AFDKSVTSTT
VADCKRACLD EKTFTCRSFN FRVSDSACDL MTHNRYTITS NQWVEDANTD YYERQCTTDQ
ENACEPGWFE WRGQCYKFSD TQSSFENASS QCQSDGGNLA SINSAEEMSF IKEKARTFYK
DKSFYIGMQW GGHGHSWIDG SSVFYSNFAH GEGRLMSITC ENNMAELDCG QGQVVRVSYA
NFGRTSLTHC NGTVQRSDCL DSTSLNTVVD TCNGIQKCSV NASGDIFSES DTCGGATRYL
EIHYNCVPAS VYSSYIVSPT GCQCYFNHSR YDCACCAAGS CQCGPSMPHK CVTCGGSCSN
TLHDHGESTC VVMSAAGDYN WYDDSCQRTD LFHVCKQARE VIAPLQCTNV IASGSNTATC
PEDAPNAVAC HCSCSNFIIK NYGRECDCSL CGTQTETLAR CCANTPPAGY DPGPDYRTFM
QCKDLPDGDP YTGVTCPADE YPTMTQCACG YCGPWWMSGN NTCSCDTSVT SDWVTGQCCR
FLFSPHDGTK PDSDTEGATY LDGRYSVK
//
