ID A0A3B3RQZ9_9TELE Unreviewed; 1374 AA.
AC A0A3B3RQZ9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Attractin {ECO:0000313|Ensembl:ENSPKIP00000020255.1};
GN Name=ATRN {ECO:0000313|Ensembl:ENSPKIP00000020255.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000020255.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000020255.1}
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; ENSPKIT00000000870.1; ENSPKIP00000020255.1; ENSPKIG00000005018.1.
DR GeneTree; ENSGT00940000157346; -.
DR OrthoDB; 5471913at2759; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR CDD; cd03597; CLECT_attractin_like; 1.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00055; EGF_Lam; 3.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR Gene3D; 2.10.25.10; Laminin; 3.
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; IPR034011; Attractin-like_CTLD.
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; IPR002049; LE_dom.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR46376:SF3; ATTRACTIN; 1.
DR PANTHER; PTHR46376; LEUCINE-ZIPPER-LIKE TRANSCRIPTIONAL REGULATOR 1; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF13854; Kelch_5; 1.
DR Pfam; PF01437; PSI; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 4.
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; 2.
DR PROSITE; PS50026; EGF_3; 2.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1224..1248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 50..82
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 84..200
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 198..235
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 747..868
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1008..1053
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DISULFID 72..81
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 202..212
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 206..223
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 225..234
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1025..1034
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1037..1051
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1374 AA; 152382 MW; D572C0BAFFB09ACF CRC64;
MTDGRRRWAC SRFGRGLSGA AAPGAPPPQH RNALLISALL FFFGPMSSTE AKECDKPCLN
GQCNPGGGNC VCEPGWVGDQ CQHCGGRFRL TGPSGFLTDG PGNYKYKTKC TWLIEGQPNT
ILRLRFNHFA TECSWDHLYV YDGDSIYAPL LAAFSGLIVP ERYSNETLPE VVSQSGYALL
HFFSDAAYNL TGFNISYRIN TCPNNCSDRG ECRPANGSAG VYCECAEQWK GEACDIPSCL
GQCGFPEWGQ CQANSSRSCL CRREWQGPDC SIPVPANRSF WTHEDYSGDS LARASHKAVV
DEDTMWVIGG YVFNYSDYKM VKAYNLTSQL WLTLNRSVDA VTARYGHSLA LHEHKIYMYG
GKIDSTGNIT NQLWVFHIHN QSWVLASPRA KEQYAVVGQS AHVVRLAQDS SVMLVIFGHC
PLYGYISKVQ EYNIATNTWS ILKTNGALVQ GGYGHSSVYD PNTSAIYIHG GYKAFSANKY
GLADDLYKYE VDTRMWTILK DSGFFRYLHT AIIVSGTMLV FGGNTHNDTS MSHGAKCFSS
DFMAYDLACD EWSVLPRPDL YHDVNRFGHS AVYSNGIMYI FGGFNSLLLS DVLTFTPASC
SAFSSETSCG SAWPGIRCLW NSSQSTCLPW EAASPHQERL VLSSCPRKAY ADNEKCDSYT
DCYSCTANTN GCQWCADQCI SMSSNCTTVT GVIAEYEMCP KDNPEYVCNK KTSCKSCAMD
QNCQWEPRNQ ECIALPENIC GESWHLVGNS CLKFITAKDS YDNAKLTCRS HNAVLASLTT
QKKVEFVLKE LQIMTVLYKA TVTPWVGLRK INISYWCWED MSPFTNTSLQ WLPGEPSDAG
FCGYLAEPAS SGLKAATCVN SVNGSLCERP ANHSAKQCRT PCALRTTCSE CTSSSSECMW
CSNMRQCVDS NAYVASFPFG QCMEWYTMNS CPPENCSGYR TCGQCLDQPG CGWCTDPSNT
GRGQCIEGSY RGPVQTPSPA SYHEPALNLT MCQQENRFNW SFIHCPVCQC NGHSRCVNES
VCEKCEDLTT GKHCESCISG YYGDPTNGGT CQPCKCNGHA SMCNPSNGKC FCTTKGIKGD
RCHLCEVENR YQGNPLKGTC YYTLLIDYQF TFSLSQEDDR YYTAINFVAT PEEQNRDLDM
FINASKNFNL NITWATSFAA GTQAGEEIPI VSRSNIKEFK DSFSNEKFDF RNNPNITFFV
YVSNFTWPIK IQIAFSQHSN FMDLVQFFVT FFSCFLSLLL VAAVVWKIKQ SCWASRRREQ
LLREMQQMAS RPFATINVAL ETDEEPPDLI GGSIKTVPKP IAMEPCFGNR AAVLSIFVRL
PRGSGGIPPP GQSGLAVASS LVDVSQQMCV AYKEKSGAVR NRKHQPPAQP ATCI
//
