ID A0A3P8Q8I4_ASTCA Unreviewed; 2773 AA.
AC A0A3P8Q8I4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Matrix-remodeling-associated protein 5-like {ECO:0000313|Ensembl:ENSACLP00000025800.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000025800.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000025800.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000025800.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR STRING; 8154.ENSACLP00000025800; -.
DR Ensembl; ENSACLT00000026412.1; ENSACLP00000025800.1; ENSACLG00000017564.1.
DR Ensembl; ENSACLT00000026424.1; ENSACLP00000025812.1; ENSACLG00000017564.1.
DR GeneTree; ENSGT00940000159942; -.
DR OMA; CNITHSS; -.
DR OrthoDB; 2918193at2759; -.
DR Proteomes; UP000265100; Chromosome 16.
DR Bgee; ENSACLG00000017564; Expressed in spleen and 3 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00096; Ig; 5.
DR Gene3D; 2.60.40.10; Immunoglobulins; 11.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
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; IPR013106; Ig_V-set.
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 InterPro; IPR000372; LRRNT.
DR PANTHER; PTHR45842:SF12; KEKKON 5, ISOFORM A; 1.
DR PANTHER; PTHR45842; SYNAPTIC ADHESION-LIKE MOLECULE SALM; 1.
DR Pfam; PF07679; I-set; 4.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13927; Ig_3; 4.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00409; IG; 11.
DR SMART; SM00408; IGc2; 11.
DR SMART; SM00406; IGv; 7.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 11.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS50835; IG_LIKE; 11.
DR PROSITE; PS51450; LRR; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..2773
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040681437"
FT DOMAIN 468..562
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 569..662
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1436..1524
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1533..1624
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1629..1719
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1867..1964
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1972..2065
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2072..2167
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2403..2497
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2575..2665
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2678..2771
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 276..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1314..1333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1364..1422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1726..1855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2179..2198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2288..2403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2541..2574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..930
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1082
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1392..1422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1726..1741
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1748..1855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2183..2198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2288..2318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2332..2403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2773 AA; 299097 MW; 0980B57ED5F88A0A CRC64;
MKMNRGVNVL AALLALLMLA LVVPTSKSCP RTCNCYQANE VHCTFRSLLA IPPGLPAHTR
RINLGFNSIR NLHDRSLAGL RRVELLMLHS NDLHHLPDAA FRDMKSLQIL KLSYNKLREI
SSSLTFSGLT SLLRLYLDHN LLQHIHPRAL LQLPSLRLLR LQGNRLHQLH PHTLCTLSLL
NTYYFSTLRH LDLSNNSLTT LPKDALATAP LLETLMLQAN PWSCDCRMNW FLSWTLAHPG
LMKCPGGPQC PLCTSPNSLQ GQGLLEQTAL TCNSPVIPSP GKEAPLGTEP SEIKSSETFR
EPLGSASLGL SDQQGYSVDL SCNITQSSDS QDIAPPPDLS VSSSSPLPLA LSLSLECPVE
RQSYEKLWRI LAYYSETAVR LEREIMLSKS PALAYRYRQA AETDGYYHTG VKASVKARPQ
WLMQPAISIQ LNRAQSNGHK VQLIYSTRVS AHLDPTSQLS SSSAASHPWV LISTNHTTTA
LAAVAGSKVQ LPCPILTSGN PKAQWILPDG SELLSPSSTL DGRLRASGFV LLLQNVQLSD
AGIYYCVARA GRDVDVLPLH LAVEESSVPH LGEQVGPPVT GTVGEPVSLP CRMSGSPEPY
LSWILPNGNV VRRGTAVPGG LTIETNGSLY LPNPSLRDGG HYRCTAVNHY GRDALSVQLI
LNSQHIPALR TSFPRGPQSA AGRSTRIRAP LLRDMNEGSG DGEEVEEATV GNRKRPVSFQ
GPPNRRYPIG NPRRRGPVRE GSRRRGGAAF SSTDQRRNLF ENKRRVSTSK KKIDPQKWAD
LLAKIRQRTA LANRGQLITT EKPTAAPVQE AEDRVTIEHE EDDDTDRGRG QAAGVEAETE
GSSVDDIVLQ EEELQPIQPV NTGSPTKTEI KTETETDSET EEGTERSTEK QIENETDTLR
QAEIPGSQTQ TAANAVTRKE PVTSYPVSGT NEIVPEPVEG DEREVNPNPS RTRPQNPRQR
FFPNLVPNSR PQRPRNSHRK IGQRRRIINR PRVQLLTPNQ RPLEPTNPIT PAVTPDTTTN
QINMLSLVST ATSAGILSTQ RDHIKTAPND VALNLFGSAS SSSSPSQTPS PSYTNRYTPT
AIMTHSGKRP DREEIPDSEE STLFSTPAPT HSNFVISETH VPGTHTLAHS IHKHTETQTA
LGKHIDTPPN KHSEKLGKNF VSILYQSSSP ATHSSLVSVS SAATAKTITN PTTAPKKVYS
NANASSSKST SSAMTNEYKL PTTTAINPRT TSSTIFARTI IPTSSTTRHT ASASTSATPI
LTPTTPATIP VVELFTTTIN PNNNALISTT TDTSTTTSSS SNSFIVTSRF LNPPSTATAS
TTSETTKTTT TTTTTPTFTV SAKIHSTSRA ATPSTLSSTA AIMTSANTKT SSRERPSIDL
ADPRERLASG APNQSRPPTD WKNAGANSIP DSHSSRTNWS PSFPVAPGAP VVRSRPRIAD
PHVRTVSFPA ESTARLTCEA KGEPKPTITW IKVATGAVMS VHSRAQRFEV LSNGTLVIQN
IQLQDRGTYI CSAQSMLGRD RLLTTLEVWT RPPRMQLASY REATIHQGGE VHLECQADGV
PAPLLSWVLP DRSVMTSAGP STSRISVDTN GTLHISVTLP SDRGVYRCVA SNSAGAASTS
VRVHVSSLPP VIQQPREEHL LLSPGRPVYA HCSARGAPPP TLRWRIPDGT LVRPSQFLHG
NLFVLTNGTL HIRKVGPKDS GSYECTASNA VGTDKRTVKL KIEGGAEGER RQGEVSHKGV
KAVATERPPS SSLINDTGLS ISNQPSNPFS SPKSPLEKSK TSLTSSSSHS SSNPYRSSNS
SPKFNKTVTA SHTHFTSVKK TNSSSLSPPS TGSINKNKVS PSITNTRVAS PTDRRASTVL
NPLLLSPFSK ARIISTSPSS STVPQGGILQ LHCSVTGNPT PIIIWRTPSR KLVDQHLSFD
RRLKVHPNGT LSVQAVTEKD AGDYLCIARN KVADDYRLLR VTVAAKPATI EPKQLLTQMV
SVGKPLKVDC QASGLPDPAV HWTLPDGTMV NSVLHGEDRG GREQRLIVFS NGTLLVPAVS
AGEGGEYTCY AENQGGHDTM KVKVKVMMTS VPTFTDDRSY HVMKVRQGAT ARIPCRATGN
PTPTVTWFNP ANRVIPRSLG SGYYFERVVV VSNGTLEVRL AQKIDTGNYT CQASNSAGER
SRVVRLEVET PTYGLRGRVE GGGWSNNSGT DTRSGDNINN GGIIRYGLSG ITDKLHNNSS
SNDNDNERIR NIVPSSGVNL AISSSNPVLK NDSQNGFNGL VSGITTKLSS SVISVGVNRA
RNVSTKADNT GINMNRPSII HNSNSVGNSR STVREGSAER NPARNINEVI AGKASNDANT
SGENGRLSGN SRNAGGFSST VSNKAVGTST HRGDDFNRSG NLGRTDSRNG GELSSNTDAK
NSPNTVLGVA TAVKQQAVKG QTIFLPCPSQ NSRQSRLFWL LPGNGMLPSP YYGSRLTVHR
NGTLELRGVR GSDGGVLVCV VRSEKGETTM RVELEVSDQQ EEVRSPHRVE RVGLTKVPLS
RGLVESEQSL SSKPASPVLY PRISVTEKPR QSAARLPSPP HPVGPPSSTG TASAPTVITQ
TASLVSIING ETLHLPCPAS QTPGFTRSSF TWTMPSGKVL SQGESDDSGR YLVQEDGALT
VQQASVFDRG TYTCRSTSYD SSSVSVITVP VIVIAYPPRI TTGPSPVTYT RPGVAVELPC
LTIATPRATV TWETPDLMQL KVMAQPRIYG NRYLSPQGSL VIQKPTSMDT GFYKCTAKNV
IGVDTKATYL HVI
//
