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Database: UniProt
Entry: A0A3Q3B6P5_KRYMA
LinkDB: A0A3Q3B6P5_KRYMA
Original site: A0A3Q3B6P5_KRYMA 
ID   A0A3Q3B6P5_KRYMA        Unreviewed;      1379 AA.
AC   A0A3Q3B6P5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Attractin like 1 {ECO:0000313|Ensembl:ENSKMAP00000024895.1};
GN   Name=ATRNL1 {ECO:0000313|Ensembl:ENSKMAP00000024895.1};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000024895.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000024895.1}
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   RefSeq; XP_017294533.1; XM_017439044.1.
DR   STRING; 37003.ENSKMAP00000024895; -.
DR   Ensembl; ENSKMAT00000025206.1; ENSKMAP00000024895.1; ENSKMAG00000018398.1.
DR   GeneID; 108249572; -.
DR   KEGG; kmr:108249572; -.
DR   CTD; 569196; -.
DR   GeneTree; ENSGT00940000155790; -.
DR   OMA; NCSMSVR; -.
DR   OrthoDB; 5471913at2759; -.
DR   Proteomes; UP000264800; 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; PF13418; Kelch_4; 1.
DR   Pfam; PF13854; Kelch_5; 1.
DR   Pfam; PF13964; Kelch_6; 1.
DR   Pfam; PF01437; PSI; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00180; EGF_Lam; 2.
DR   SMART; SM00612; Kelch; 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; 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:UP000264800};
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        1229..1253
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          80..196
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          194..232
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          746..866
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1013..1058
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1352..1379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        198..208
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        222..231
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1030..1039
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1042..1056
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   1379 AA;  151973 MW;  D9C2E0E3837F62EF CRC64;
     MDRGGQREPG LFPPGPKLAR DTSDPRGLNK YLVAYVLLSF ALLAHASPAK PCDKNCLSGK
     CVNGSCVCDR GWVGDLCQHC QGRFRLTEPS GYLTDGPINY KYKTKCTWLI EAYPNAVLRL
     RFNHFATECS WDHMYVYDGD SVYAPLVAVF SGLIVPEIRG NETVPEVETT SGYALLHFFS
     DAAYNLTGFE IFYSINSCPN NCSGHGKCTP GNSAASRVYC ECDKYWKGEA CDIPYCRNNC
     GSPDHGYCDL TGEKLCVCND SWQGPDCSLT VPSTESFWVL PSVKPFGTSL ARASHKAVVQ
     EKTMWVVGGY TFNYSSFQMI LNYNLESGVW NTVPSSGGPV PRYGHSLAAH QDKIYMFGGK
     LEASWGNVTD ELWTFNVSSR TWQRGHPEVD SQAQAQIYAV EGHTAHCVQL SSGETIMLVI
     FGFSPIYSYI SNVQEYNLKS NKWLVPETKG AIPQGGYGHT STYDSASGSI YVHGGYKALP
     ANKYGLVDDL YRYDVNTRTW FILRESSFPR YLHSAVLLSG TLLVFGGNTH NDTSLSNGAK
     CFSADFLAYD IACDEWRLLP KPDLHRDVNR FGHSAVVSNG SMYVFGGFSS VLLNDVLVYR
     PPSCQAFSTE EGCAKAGPGV RCLWSRGRCL PWEPSMANGS LTPAPFCPSK PATVDEWCYR
     FSDCGSCTAN TKGCQWCDDK KCISASSNCT SNVKNFTMCP VRNEQVCSKL ANCKSCSLNL
     NCHWDQNHSQ CLALPAQQCS DGWSQVGDAC LRINSSRESY DNAQHYCKNL NGNIASLTTF
     KQVHFVLQEL KKLQEEDKRL SPWVGLRKIN VSYWGWEDMT PFTNSTLHWL PGEPSDSGFC
     AYLEEPQASG LKANPCTATA HGLICEKATG NPSQSTRSSC KKPCALHTNC ANCTSQAMEC
     MWCGSTQRCV DSTAYVISFP YGQCLEWQTA DCVAQNCSGL RTCSQCLEQP ECGWCGDPSS
     TGKGLCMEGS YRGPMKRLSK QGQHSLSYDM SLEPGSCPKD KGFEWAFIHC PACQCNGHST
     CVNGSVCEQC RNLTTGPHCE TCMPGYHGDP TNGGKCQACK CNGHANVCQV LTGKCFCTTK
     GIKGDQCQLC DSENRYLGNP LRGTCYYNLL IDYQFTFSLI QEDDNHYTAI NFMASPEQAN
     KNLDMSINAS NNFNLNITWS VGSTAGTISG EEVPIVSKTN IKEYRDSFSC EKFTFRSNPN
     ITFYVYVSNF SWPIKIQIAF SQHSSIMDLV QFFVTFFSCF LSLLLVAAVV WKIKQTCWAS
     RRREQLMRER QQMASRPFAS VAVSLDARGE LTEVLQPMVD GMPKPVAMEP CSGGKAAVLT
     VLMRLPSGPS GLPPPGQSGL IVASALIDVS QQKPSDFKDK SQALKNRKAL PPAHQGTCV
//
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