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Database: UniProt
Entry: K7F0Z4_PELSI
LinkDB: K7F0Z4_PELSI
Original site: K7F0Z4_PELSI 
ID   K7F0Z4_PELSI            Unreviewed;       521 AA.
AC   K7F0Z4;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Adhesion molecule with Ig like domain 2 {ECO:0000313|Ensembl:ENSPSIP00000001704.1};
GN   Name=AMIGO2 {ECO:0000313|Ensembl:ENSPSIP00000001704.1};
OS   Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC   Trionychidae; Pelodiscus.
OX   NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000001704.1, ECO:0000313|Proteomes:UP000007267};
RN   [1] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG   Soft-shell Turtle Genome Consortium;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
RN   [3] {ECO:0000313|Ensembl:ENSPSIP00000001704.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. AMIGO family.
CC       {ECO:0000256|ARBA:ARBA00005670}.
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DR   EMBL; AGCU01109011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006126534.1; XM_006126472.2.
DR   AlphaFoldDB; K7F0Z4; -.
DR   STRING; 13735.ENSPSIP00000001704; -.
DR   Ensembl; ENSPSIT00000001709.1; ENSPSIP00000001704.1; ENSPSIG00000001708.1.
DR   GeneID; 102460204; -.
DR   KEGG; pss:102460204; -.
DR   CTD; 347902; -.
DR   eggNOG; ENOG502R009; Eukaryota.
DR   GeneTree; ENSGT00950000183146; -.
DR   HOGENOM; CLU_030478_0_0_1; -.
DR   OMA; QKNMLNQ; -.
DR   OrthoDB; 3789698at2759; -.
DR   TreeFam; TF326838; -.
DR   Proteomes; UP000007267; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   InterPro; IPR031283; AMIGO.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013151; Immunoglobulin.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR24368; AMPHOTERIN-INDUCED PROTEIN; 1.
DR   PANTHER; PTHR24368:SF209; AMPHOTERIN-INDUCED PROTEIN 2; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   PRINTS; PR00019; LEURICHRPT.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00369; LRR_TYP; 5.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51450; LRR; 1.
PE   3: Inferred from homology;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           39..521
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003903607"
FT   TRANSMEM        398..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          302..382
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   REGION          434..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          499..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        437..454
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   521 AA;  58204 MW;  E0FFD2CB56DF0116 CRC64;
     MSLSCQTIST RLGVLTLNCK GLLCLLVFTL SVSGSASGLC PTACICASDI ISCTNKNLSR
     VPGTLFKFIK RLDLSYNKIG FLEPEWVPVL FDKLNTLIIS HNSISSIITG SFSTTPNLKY
     LDLSSNNLKT LGSPLFQELR VLEVLLLYNN QITQIDSAAF GGLYKLQKLY LCCNSLSHFP
     MDLYIGKHKL TELVLLDISY NHIQSVPIQR VSLVPAKQLS GIYLHGNPFY CDCTLYSMLI
     FWYHRHFNSV VDFKNEYACA LRSDPKGSNK LPLLHDNFLN CSESTINVSF HAFGFIYEAQ
     VGERLIVHCD SKISDAGTYF IWVSPDNRLL EPDKETDSFK VFHNGSLEII DPQLEDSGLY
     SCVAINKRRL LNETIEVRIN VSNFTVNRSH AHEAFNTAFT TLAACVASII LVLLYLYLTP
     CPCQCKTRRR KRKLPQSSAH SSILNSTPPL DPPTEEKKSS TGKRVVFLEP VNEPKQGQNG
     KVRLFSKETV IAESILKTTR AKSDSDSVNS VFSDTPFMPS S
//
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