ID A0A671X3R9_SPAAU Unreviewed; 1291 AA.
AC A0A671X3R9;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Attractin-like protein 1 {ECO:0000313|Ensembl:ENSSAUP00010045782.1};
GN Name=LOC115596686 {ECO:0000313|Ensembl:ENSSAUP00010045782.1};
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:ENSSAUP00010045782.1, ECO:0000313|Proteomes:UP000472265};
RN [1] {ECO:0000313|Ensembl:ENSSAUP00010045782.1}
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; ENSSAUT00010048128.1; ENSSAUP00010045782.1; ENSSAUG00010018310.1.
DR GeneTree; ENSGT00940000155790; -.
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; 2.
DR Pfam; PF13415; Kelch_3; 1.
DR Pfam; PF01437; PSI; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 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.
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 Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000472265};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..42
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 43..1291
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025432818"
FT DOMAIN 77..193
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 191..229
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 776..896
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 195..205
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 219..228
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1291 AA; 143283 MW; CD75100A1ED08EDA CRC64;
MDDVGGVHLC AWTRSSRRSA RDALRTYLAV FVMLHLVLHT EGSTVSKSCD KSCYSGKCMN
GTCVCDHGWV GDQCQHCQGR FKLTDLTGFL TDGPVNYKYK TKCTWLIEGY PNAVLRLRFN
HFATECSWDH MYVYDGDSIY APLIAVFSGL VVPETRGNET VPEVVTTSGY ALLHFFSDAA
YNLTGFNIAY SINSCPNNCS GHGRCSTANS VSGRVYCECE DYWKGDACNI PYCRDNCGSP
DHGYCDLTGE KLCVCNDSWQ GPDCSLSVPS TEAFWVLPSV KPSAQSLGRA SHQALVHSGL
MWVVGGYSFN YSNYHMVLNY NLESSTWDVV PVSSGPLYRY GHSLALHQDD IYMFGGKLEA
KSANVTDELW VFNIPRRTWS PRKPAPPPPY ALEGHTAHVV ELANGEPVML IFFGYSPIYS
YINKVQEYNI RSNSWQVVSA GGAVVQGGYG HSSVYDEASG CVFVHGGYKA LSNNKYGLVD
HMYRYHVHTK TWLILGESGL ARYLHSAVVL SGTLLVFGGN THNDTSLSNG AKCFSADFMA
YDIACDEWTV LPRPGLHRDV NRFGHSAVVS NGSMYIFGGF SGLLLNDVLA YTPPSCLAFS
NPTSCAAAGP GLRCLWVQSR CLPWEPKPPE YTLPATFCPA RPDSTDEQCF RFSDCASCTA
NTRGCQWCED RKCISTSSNC TVLTLELAQQ HGGALSLSPP PSMLSEHQLS LWKHGGRRRG
HSVTDSSRCK RREEQECFRL ANCRSCSLNT NCQWEMQQQE CQALPGQLCG EGWHHVGEAC
LRINSSRESY DNAQHYCKNL GGNIASLLTD KQVNFVLEEL QKYQLQDKTL SPWVGLRKIN
VSYWGWEDMS PFTNTSLRWL PGEPSDSGFC AYLERAHVAG LKANPCTATS DGLICEKPAG
SPQSQSARPC KTPCSLRTSC ANCTSQAMEC MWCSSTQRCV DSSAYVISFP YGQCLEWQTQ
DCSAQNCSGL RTCSDCLERA ECGWCGDPSN TGKGVCMEGS YRGPLKPAGA RTGPRDRDRL
RDRDMVLDQS LCTSDRGYNW AFIQCPACQC NGHSRCVNGS VCEHCGNLTA GTHCQSCMAG
YYGDPINGGK CNACKCNSHA NVCHVNSGKC FCTTKGIKGD QCQLCDSENR YLGNPLRGTC
YYNLLIDYQF TFSLLQEDDR YYTAINFMAT PEQANKNLDM SINASNNFNL NITWSFSSTA
GTISGEEMPI IARTNIKEHR DSFSCEKFDF RLHHNITFYV YVSNFSWPIK IQIAFSQHNS
IMDLVQFFVT FFRTEETGSD RSSRTRNTMK N
//
