ID W5KWZ0_ASTMX Unreviewed; 1365 AA.
AC W5KWZ0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Attractin like 1 {ECO:0000313|Ensembl:ENSAMXP00000012102.2};
GN Name=ATRNL1 {ECO:0000313|Ensembl:ENSAMXP00000012102.2};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000012102.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000012102.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; ENSAMXT00000012102.2; ENSAMXP00000012102.2; ENSAMXG00000011688.2.
DR eggNOG; KOG1388; Eukaryota.
DR GeneTree; ENSGT00940000155790; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000011688; Expressed in camera-type eye and 14 other cell types or tissues.
DR GO; GO:0016020; C:membrane; 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; 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; PF13415; Kelch_3; 1.
DR Pfam; PF13854; Kelch_5; 2.
DR Pfam; PF01437; PSI; 2.
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; 4.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1215..1239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 81..194
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 192..230
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 741..860
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 999..1044
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DISULFID 196..206
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 220..229
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1016..1025
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1028..1042
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1365 AA; 151121 MW; 879ED019FB845FED CRC64;
MDAAKMFRTE LFAFRRRQDA LTCFRLQGMN TYLLLCAMFS LVLLTDASPS KTCEKNCLSG
KCVNGSCVCD RGWVGDQCQH CQGRFKLTEP SGYLTDGPIN YKYKTKCTWL IEGYPNAVLR
LRFNHFATEC SWDHMYVYDG DSIYAPLVAV AIDPEPEDDE WLPEVETNSG YALLHFFSDA
AYNLTGFDIF YSINSCPNNC SGHGKCTTSN SIASRVYCEC DKYWKGEACD IPYCRNNCGS
PDHGYCDLTG EKLCVCNDSW QGPDCSLTVP STESYWVMPT VKPFGTSLGR ASHKAVVQEK
VMWVVGGYTF NYSNFQMILN YNLDTGTWNT VASSSGPLSR YGHSLTLYQD DLYMFGGKLE
MGSGNVTDEL WVFNIPSKSW SLRTPSTPAH GQVYAVEGHS AHIAELDTGD VVMVVIFGYS
SIYSYISNVQ EYNIRTNTWL VPETKGATVQ GGYGHSSVYD SGSKSVYVHG GYKSLPANKY
SLVDDLYRYE VHTRIWTILK ESGSPRYLHS AVLLGGTLLI FGGNTHNDTS LSNGAKCFSA
DFLAYDIACD EWKVLPRPNL HRDVNRFGHT AVTSNGSMYV FGGFSSVLLN DVLIYRPPSC
EAFLGQERCE AAGPGVRCVW RKTRCISWEP SFTSNTIPAA FCPAKPAPVD ERCHRFSDCT
SCTANTNGCQ WCDDKKCISA LSNCTASVKN FTKCSIRNEQ ICSKLANCKS CSLNLNCQWD
HQQHECHALP AKLCGDGWSH VGEACLRINS SRDSYDNARH YCKNLGGIIA SLSTAKQVDF
ILEELQKYQQ QEKLSPWVGL RKINVSYWGW EDNSPFTNTS LQWLPGEPND SGFCAYLEKA
QVSGLRANPC NANTDGLICE KGVESRNARP CKMPCSLHVT CENCTSQATE CMWCGSTKRC
VDSNAYVISF PYGQCLEWQT GDCVSQNCSG FRTCGHCLEQ PDCGWCGDPS NTGRGQCVEG
SYRGPMKNPP KHSQDMVLDT GLCPKERGFE WAFIQCPACQ CNGHSTCVNG SVCEQCRNLT
TGPHCETCMA GYHGDPTNGG KCQACKCNGH ANVCQVLTGK CFCTTKGIKG DQCNLCDSEN
RYLGNPLRGT CYYNLLIDYQ FTFSLLQEDD HYYTAINFMA TPEQTNKNLD MSINASNNFN
LNITWSVGST AGTISGEEVP IVSKTNIKEH RDSFSCEKFS FRSNPNITFY VYVSNFSWPI
KIQIAFSQHN SIMDLVQFFV TFFSCFLSLL LVAAVVWKIK QTCWASRRRE QLMRERQQMA
SRPFASVAMA LDVGGGQVDL LQGGIEGPPK PVAMEPCSGG KAAVLTVLLC LPQGPSGVPP
PGQSGIAIAS ALIDTSQQKP MDFKEKNQGL KNRKALPTAH QGTCV
//