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Database: UniProt
Entry: A0A671WU99_SPAAU
LinkDB: A0A671WU99_SPAAU
Original site: A0A671WU99_SPAAU 
ID   A0A671WU99_SPAAU        Unreviewed;      1381 AA.
AC   A0A671WU99;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Attractin like 1 {ECO:0000313|Ensembl:ENSSAUP00010042264.1};
GN   Name=ATRNL1 {ECO:0000313|Ensembl:ENSSAUP00010042264.1};
OS   Sparus aurata (Gilthead sea bream).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Spariformes; Sparidae; Sparus.
OX   NCBI_TaxID=8175 {ECO:0000313|Ensembl:ENSSAUP00010042264.1, ECO:0000313|Proteomes:UP000472265};
RN   [1] {ECO:0000313|Ensembl:ENSSAUP00010042264.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   Ensembl; ENSSAUT00010044490.1; ENSSAUP00010042264.1; ENSSAUG00010017716.1.
DR   GeneTree; ENSGT00940000155790; -.
DR   OrthoDB; 5471913at2759; -.
DR   Proteomes; UP000472265; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   CDD; cd00041; CUB; 1.
DR   CDD; cd00055; EGF_Lam; 1.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR002049; LE_dom.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   PANTHER; PTHR46376:SF2; DISTRACTED, ISOFORM B; 1.
DR   PANTHER; PTHR46376; LEUCINE-ZIPPER-LIKE TRANSCRIPTIONAL REGULATOR 1; 1.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF01344; Kelch_1; 1.
DR   Pfam; PF13418; Kelch_4; 1.
DR   Pfam; PF13964; Kelch_6; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF01437; PSI; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00180; EGF_Lam; 2.
DR   SMART; SM00423; PSI; 5.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF117281; Kelch motif; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS01180; CUB; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 1.
DR   PROSITE; PS50027; EGF_LAM_2; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW   Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW   ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Lectin {ECO:0000256|ARBA:ARBA00022734};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472265};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        29..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1231..1255
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          81..197
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          195..233
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          747..867
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1015..1060
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   REGION          975..995
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1356..1381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        980..995
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        199..209
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        223..232
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1032..1041
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1044..1058
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   1381 AA;  152486 MW;  84E51FD4527369C0 CRC64;
     MDPGGECTTR LFLFLFGPRL ATHSHLRGIN RYLVVYVLFY FVLFTHASPA KPCDKSCLSG
     KCINGSCICD RGWVGDQCQH CQGRFKLTEP SGYLTDGPIN YKYKTKCTWL IEGYPNAVLR
     LRFNHFATEC SWDHMYIYDG DSIYAPLVAV FSGLIVPEIR GNETVPEVET TSGYALLHFF
     SDAAYNLTGF EIFYSINSCP NNCSGHGKCT PGNSAASRVY CECDKYWKGE ACDIPYCRNN
     CGSPDHGYCD LTGEKLCVCN ESWQGPDCSL TVPSTESFWV LPSVKPFGTS LARASHKTVV
     QEKVMWVVGG YTFNYSSFQM ILNYNLESGI WNTVPINSGP VPRYGHSLAA YQDDIYMFGG
     KLEAGWGNVT DELWVFNMPS RTWQRRNPVM GPPAQAQIYA VEGHSAHCAL LDGGEAIMLV
     IFGYSPIYSY ISNVQEYNLR SNTWLVPETK GAVPQGGYGH SSTYDSASGS VYVHGGYKAL
     PANKYGLVDD LYRYEVNTRT WLILRESGFP RYLHSAALLS GTLLVFGGNT HNDTSLSNGA
     KCFSADFLAY DIACDEWSLL PKPDLHRDVN RFGHSAVVSN GSMYVFGGFS GVLLNDVLVY
     RPPSCQAFLA EEGCVKAGPG VRCIWSRGRC LPWEPSMANG SLLPAPFCPT KAVTVDERCY
     RFSDCASCTA NTNGCQWCDD KKCISASSNC TSNVKNFTEC PVRNEQVCSK LANCKSCSLN
     LNCQWDQNQS ECHALPAQQC SEGWNQVGEA CLRINSSRES YDNAQHYCKN LNGNIASLTT
     SKQVDFVLEE LKKLQEQDKR LSPWVGLRKI NVSYWGWEDM SPFTNSSLRW LPGEPSDSGF
     CAYLEEPQVS GLRANPCTAT AHGLICEKAT GNPNQSSRPS CKKPCSLHTT CTNCTSQAME
     CMWCGSAQRC VDSTAYVISF PYGQCLEWQT GDCVAQNCSG LRTCSQCLEQ PECGWCGDPS
     STGKGLCMEG SYRGPMKRPV KQGQQSQQSQ DMSLEPGSCP KDKGYEWAFI HCPACQCNGH
     STCVNGSVCE QCRNLTTGPH CQTCMPGYHG DPTNGGKCQA CKCNGHASVC QVLTGKCFCT
     TKGIKGDQCQ LCDSENRYLG NPLRGTCYYN LLIDYQFTFS LIQEDDNHYT AINFMASPEQ
     ATKNLDMSIN ASNNFNLNIT WSVGSTAGTI SGEELPIMSK TNIKEYRDSF SCERFTFRSN
     PNITFYVYVS NFSWPIKIQI AFSQHNSIMD LVQFFVTFFS CFLSLLLVAA VVWKIKQTCW
     ASRRREQLMR ERQQMASRPF ASVAVALDAR GEQTELLQHV VDGAPKPVAM EPCSGGKAAV
     LTVLLRLPSG PSGLPPPGQS GIIVASALID VSQQKPTDFK DKSQALKSRK ALPPAHQGTC
     V
//
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