ID A0A3P9N4U2_POERE Unreviewed; 434 AA.
AC A0A3P9N4U2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Matrix remodeling-associated protein 8 {ECO:0000256|ARBA:ARBA00018734};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000004589.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000004589.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000004589.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
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DR RefSeq; XP_008407503.1; XM_008409281.2.
DR AlphaFoldDB; A0A3P9N4U2; -.
DR Ensembl; ENSPRET00000004653.1; ENSPREP00000004589.1; ENSPREG00000003226.1.
DR GeneID; 103464890; -.
DR KEGG; pret:103464890; -.
DR GeneTree; ENSGT00390000001509; -.
DR OrthoDB; 4235152at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000003226; Expressed in head and 1 other cell type or tissue.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
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; IPR013106; Ig_V-set.
DR InterPro; IPR042472; MXRA8.
DR PANTHER; PTHR44793; MATRIX REMODELING-ASSOCIATED PROTEIN 8; 1.
DR PANTHER; PTHR44793:SF1; MATRIX REMODELING-ASSOCIATED PROTEIN 8; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638};
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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..434
FT /note="Matrix remodeling-associated protein 8"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018128672"
FT TRANSMEM 334..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..159
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 180..293
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
SQ SEQUENCE 434 AA; 49925 MW; 845A766845EA6491 CRC64;
MIMRDAVILQ ALLFIHISVA CFFTAVSCQS DSSSSVVVAG YNVSGPAGSN LVLQCMSGRM
VWTRDRVRDR QRVVHWDMYR DTPDFAMERV VDMFPAGDQR LYHTHNLRRI SLNPTAFKDG
NFSLVIKDVR MNDRGLYSCN LHHLYCHLHE TVRVQLNVTK SKRKQQRFWD GQKAVYVVLQ
GTTAVLPCIN RRSVWTDWSD EEEDQQVVHW DRQSPGVQHD SADRLVDLYA SGEQRSYGPL
FLQRKMNISN KAFSEGDFSL TITDLQLTDQ GTYSCHLHHH YCGLHERRQF RVTVEAPLIR
STQPVVTLSR DKDSSKADAP RVINVILPDQ KHHFLLPLVY VLASFLLLAS FTLVVVLVMK
RRRKAKDFSP KVSVRSSRSP SSSDEYEIDI GEVDTCTQEE KGFEYKNNLL KENVLMKTQP
KVIDLDKEIQ KFSK
//
