ID A0A3B4VIB0_SERDU Unreviewed; 1299 AA.
AC A0A3B4VIB0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Attractin like 1 {ECO:0000313|Ensembl:ENSSDUP00000030691.1};
GN Name=ATRNL1 {ECO:0000313|Ensembl:ENSSDUP00000030691.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000030691.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000030691.1}
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; ENSSDUT00000031226.1; ENSSDUP00000030691.1; ENSSDUG00000022073.1.
DR GeneTree; ENSGT00940000155790; -.
DR Proteomes; UP000261420; 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; PF13854; Kelch_5; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF01437; PSI; 2.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00180; EGF_Lam; 2.
DR SMART; SM00612; Kelch; 3.
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 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 1149..1173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..116
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 114..152
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 666..786
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 933..978
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT REGION 1274..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 118..128
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 142..151
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 950..959
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 962..976
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1299 AA; 143283 MW; 09E7E8A47D70B251 CRC64;
MLPLKLMEPS GYLTDGPINY KYKTKCTWLI EGYPNAVLRL RFNHFATECS WDHMYVYDGD
SIYAPLVAVF SGLIVPEIRG NETVPEVETT SGYALLHFFS DAAYNLTGFE IFYSINSCPN
NCSGHGKCTP GNSVASRVYC ECDKYWKGEA CDIPYCRNNC GSPDHGYCDL TGEKLCVCND
SWQGPDCSLT VPSTESFWVL PSVKPFGTSL ARASHKAVVQ EKVMWVVGGY TFNYSSFQMI
LNYNLESGTW NTVPINSGPV PRYGHSLAAY QDDIYMFGGK LEAGWGNVTD ELWVFNVPSR
TWQRRTPVVG PPAQAQIYAV EGHSAHCVLL EGGEAIMLVI FGYSPIYSYI SNVQEYNLRS
NTWLVPETKG AIPQGGYGHT STYDSSSGSV YVHGGYKALP ANKYGLVDDL YRYDVNTRTW
FILRESGFPR YLHSAVLLSG TLLIFGGNTH NDTSLSNGAK CFSADFLSYA IACDEWRLLP
KPDLHRDVNR FGHSAVVSNG SMYVFGGFSG VLLNDVLVYR PPSCQAFLAE EGCVKAGPGV
RCIWSRGRCL PWEPSMANGS LTPAPLCPPK PVTVDERCYR FSDCASCTAN TNGCQWCDDK
KCISASSNCT SNVRNFTECP VRNEQVCSKL ANCKSCSLNL NCQWDQNQPE CHALPAQQCS
EGWSQVGEAC LRINSSRESY DNAQHYCKNL NGNIASLTTS KQVDFVLEEL KKLQQQEKRL
SPWVGLRKIN VSYWGWEDMS PFTNSSLRWL PGEPSDSGFC AYLEEPQVSG LRANPCTATA
HGLICEKATG NPNQSTRPSC KKPCSLHTNC ANCTSQAMEC MWCGSAQRCV DSTAYVISFP
YGQCLEWQTG DCVAQNCSGL QTCSQCLEQP ECGWCGDPSS TGKGLCMEGS YRGPMKRTAK
QGQQGQSQDM SLEPGSCPKD KGYEWAFIHC PACQCNGHST CVNGSVCEQC RNLTTGPHCQ
TCMPGYHGDP TNGGKCQACK CNGHASVCQV LTGKCFCTTK GIKGDQCQLC DSENRYLGNP
LRGTCYYNLL IDYQFTFSLI QEDDNHYTAI NFMASPEQAN KNLDMSINAS NNFNLNITWS
VGSTAGTISG EEVPIVSKTN IKEYRDSFSC EKFTFRSNPN ITFYVYVSNF SWPIKIQIAF
SQHNSIMDLV QFFVTFFSCF LSLLLVAAVV WKIKQTCWAS RRREQLMRER QQMASRPFAS
VAVALDARGE ETELLQPVVD GVPKPVAMEP CSGGKAAVLT VLMRLPSGPL GLPPPGQSGL
IVASALIDIS QQKPSDFKDK SQALKNRKAL PPAHQGTCV
//
