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Database: UniProt
Entry: A0A401PT70_SCYTO
LinkDB: A0A401PT70_SCYTO
Original site: A0A401PT70_SCYTO 
ID   A0A401PT70_SCYTO        Unreviewed;       742 AA.
AC   A0A401PT70;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Ig-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=scyTo_0018330 {ECO:0000313|EMBL:GCB76346.1};
OS   Scyliorhinus torazame (Cloudy catshark).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC   Scyliorhinus.
OX   NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB76346.1, ECO:0000313|Proteomes:UP000288216};
RN   [1] {ECO:0000313|EMBL:GCB76346.1, ECO:0000313|Proteomes:UP000288216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA   Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA   Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA   Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA   Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT   "Shark genomes provide insights into elasmobranch evolution and the origin
RT   of vertebrates.";
RL   Nat. Ecol. Evol. 2:1761-1771(2018).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GCB76346.1}.
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DR   EMBL; BFAA01012660; GCB76346.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401PT70; -.
DR   STRING; 75743.A0A401PT70; -.
DR   OMA; PYLAPHH; -.
DR   Proteomes; UP000288216; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR45842:SF3; LEUCINE-RICH REPEAT AND FIBRONECTIN TYPE-III DOMAIN-CONTAINING PROTEIN 4; 1.
DR   PANTHER; PTHR45842; SYNAPTIC ADHESION-LIKE MOLECULE SALM; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00369; LRR_TYP; 6.
DR   SMART; SM00082; LRRCT; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288216};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..742
FT                   /note="Ig-like domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019137185"
FT   TRANSMEM        523..549
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          289..375
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          416..512
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          391..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..409
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        596..616
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..676
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   742 AA;  81458 MW;  0B4A7B7345B3F26D CRC64;
     MERLLLVLLL SGGLAAVAEA CPFHCTCQNL SESLSTLCAN KGLLFIPVNI DRRTVELRLA
     DNFIRTVEQQ DFLNMSGLVD LTLSRNTIRF IQPFAFGDLE SLRSLHLDSN RLTAIQDDNL
     SGMVNLQHLI INNNQLISIV ETAFDDFVLT LEDLDLSFNN LQTVPWEAIQ SMVNLHMLNL
     DHNLIDYVMA GTFAELFKLA RLDMTSNRLQ TLPPDSLFAR SQTGVISPTP YTSTITLNFG
     GNPLHCNCEL LWLRRLVRED DMETCATPSH LAGKYFWYIP EEEFICEPPL ITRHTHKIWI
     LEGQRATLKC RAIGDPEPII HWVSPEDKIV SNSSRMTSYR NGTLDILVAT VRDDGSYTCF
     ATNAAGESTA LADLKIIPLP HRGNGTVRVL HRDPGSSDIT TSNKPAINGT DGRRRQEKTV
     TVVDVTATTA LVRWPSAKPP HGVWMYQIQY NSSVDETLVY RIIASTSKAF VLKNLISGAD
     YDLCILAIYG DTVTQLAATK VVGCAQFGTK EEYPHCHLLH AHFLGGTLTV IVGGIIVVTL
     LVFTVAMMVK YKICGSAHSP KVSDVYSQTN GSQSIANGML SRRRVMVLHS AGQPADKAMP
     PPPPPSSCAP PPPSRVKPPR KRFRSRPRGE GGERPPAGGH ARQGPGPRAG VPPPGDTPTS
     TSPASDQLSP AAAATSRAKR SCSFDMGDIA ATTCYSYAKR FSVIWTKRSQ SVHGMLLQYA
     ETEVTGKKGA FYSSEELEES IV
//
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