ID A0A091WBN4_OPIHO Unreviewed; 1290 AA.
AC A0A091WBN4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Attractin {ECO:0000313|EMBL:KFQ99135.1};
DE Flags: Fragment;
GN ORFNames=N306_08774 {ECO:0000313|EMBL:KFQ99135.1};
OS Opisthocomus hoazin (Hoatzin) (Phasianus hoazin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae;
OC Opisthocomus.
OX NCBI_TaxID=30419 {ECO:0000313|EMBL:KFQ99135.1, ECO:0000313|Proteomes:UP000053605};
RN [1] {ECO:0000313|EMBL:KFQ99135.1, ECO:0000313|Proteomes:UP000053605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N306 {ECO:0000313|EMBL:KFQ99135.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR EMBL; KK733764; KFQ99135.1; -; Genomic_DNA.
DR STRING; 30419.A0A091WBN4; -.
DR PhylomeDB; A0A091WBN4; -.
DR Proteomes; UP000053605; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00055; EGF_Lam; 2.
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:SF3; ATTRACTIN; 1.
DR PANTHER; PTHR46376; LEUCINE-ZIPPER-LIKE TRANSCRIPTIONAL REGULATOR 1; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF01344; Kelch_1; 1.
DR Pfam; PF13964; Kelch_6; 1.
DR Pfam; PF01437; PSI; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00042; CUB; 1.
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; PS01186; EGF_2; 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:UP000053605};
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 1140..1164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..113
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 111..148
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 660..780
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 924..969
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DISULFID 115..125
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 119..136
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 138..147
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 941..950
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 953..967
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ99135.1"
FT NON_TER 1290
FT /evidence="ECO:0000313|EMBL:KFQ99135.1"
SQ SEQUENCE 1290 AA; 143887 MW; 004104F179AA8084 CRC64;
YRLTGPSGYV TDGPGNYKYK TKCTWLIEGR PNTILRLRFN HFATECSWDH LYVYDGDSIY
APLLAAFSGL IVPEKDSNET VPEVVATSGY ALLHFFSDAA YNLTGFNITY NFNMCPNNCS
GRGECRLNNS SGALECECAK YWKGEACDVP YCADDCGAPE RGHCNPNDTK ACLCSAGWQG
PGCSIPVPAN QSFWTREEYS LPKLPRASHK TVIHDNKMWI VGGYVFNHSD SQKVLAYDLI
SEEWLPLDNT VNSVEMRYGH SLALHKDDIY MYGGKIDATG NVSSQLWVFH IPTQTWAQAT
PKAKEQYAVV GHSAHIVTLE DNSTVMLVIF GHCPLYGYIS NVQEYNLDTN TWNVLQTSGA
LVQGGYGHSS VYDPNTRSIY IHGGYKAFSA NKYRLADDLY RYEVDSRMWT ILKDSRFFRY
LHTAVIMSGT MLVFGGNTHN DTSMSHGAKC FSSDFMAYDI ACDRWAVLPR PGLHHDVNRF
GHSAVLYNST MYVFGGFNSL LLSDILKYTP ERCEAFDNET ACLRAGPGVR CVWAPSPPRC
VPWEMATVEQ QQKVFEDCPP KPVVDNEKCD QITDCYSCTA NTNNCQWCTD QCISMQNNCT
EEQVPVTLYD NCPKDNPAYY CNKKTSCKSC AMDQNCQWEP RNQECIALPE NICGTNWHLV
GNSCLRITNA KENYDHAKLS CRSNGALLAS LTTQKKVEFV LKELQKMQSS PKTLTPWVGL
RKINVSYWCW EDMSPFTNTL LQWLPDEPSD AGFCGYLAEP FLQGLKAATC INEVNGSVCE
RPANHSAKQC RTPCALRTVC GECTSGSSEC MWCSNMKQCV DSNAYVASFP YGQCMEWYTM
SSCPPENCSG YCTCAHCLEQ PGCGWCTDPS NTGKGKCIEG SYRGPVKMPT PAAPGKHGLE
PTLNVSMCPV ENSYNWSFIQ CPVCQCNGHS KCVNESICEK CENLTTGKHC ETCISGYYGD
PTNGGTCQPC KCNGHASVCN TNTGKCFCTT KGIKGDECQL CEVENRYQGN PLKGTCYYTL
LIDYQFTFSL SQEDDRYYTA INFVATPEEQ NRDLDMFINA SKNFNLNITW STSFAAGTQA
GEEIPVVSRT NIKEYKDSFS NEKFDFRNNP NITFFVYVSN FTWPIKIQIA FSQHSNFMDL
VQFFVTFFSC FLSLLLVAAV VWKIKQSCWA SRRREQLLRE MQQMASRPFA SINVALETDE
EPPDLIGGSI KTVPKPIALE PCFGNKAAVL SVFVRLPRGL GGIPPPGQSG LAVASALVDI
SQQMPIAYKE KSGAIRNRKQ QPPAQPGTCI
//
