ID A0A3B5PZ20_XIPMA Unreviewed; 1203 AA.
AC A0A3B5PZ20;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=MAM domain containing 4 {ECO:0000313|Ensembl:ENSXMAP00000022941.1};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000022941.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000022941.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000022941.1};
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:PRU00124}.
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DR AlphaFoldDB; A0A3B5PZ20; -.
DR Ensembl; ENSXMAT00000038637.1; ENSXMAP00000022941.1; ENSXMAG00000003055.2.
DR GeneTree; ENSGT00940000164732; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 2.
DR CDD; cd06263; MAM; 5.
DR Gene3D; 2.60.120.200; -; 6.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR000998; MAM_dom.
DR PANTHER; PTHR23282; APICAL ENDOSOMAL GLYCOPROTEIN PRECURSOR; 1.
DR PANTHER; PTHR23282:SF146; ENDOSOMAL GLYCOPROTEIN PRECURSOR, PUTATIVE-RELATED; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF00629; MAM; 6.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00192; LDLa; 3.
DR SMART; SM00137; MAM; 5.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 6.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 2.
DR PROSITE; PS50060; MAM_2; 6.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW Signal {ECO:0000256|SAM:SignalP}; 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..1203
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017265583"
FT TRANSMEM 1124..1146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 55..221
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 268..431
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 455..625
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 635..784
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 786..946
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 949..1109
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT REGION 1172..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 14..26
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 33..48
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 230..242
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 237..255
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 249..264
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1203 AA; 132217 MW; 9C1532BA46F5D0BA CRC64;
MLRFWSSTIL LLFCLQRVCA SGSSRCETPE GKCDFVCDCS DCSDEQNCGY SGKSFECDFE
DEGVCGWRIE SVGEEYKWQR VQSGGELPES GPTSDYTTGT ATGWFMSVSA VGAESLQSSV
LISPEIKGSS PTCRLRLRYS LWDSGLTGLG PTPLWASILH QDSQKAVVWR PETSSARSWR
EATVFLGRIS SPFRIHLHSA RSAGQNGDVA IDQLEFLDCA LPSLPAGTSC PEGMVQCGGG
GCVEQRQVCD GTDDCGDGSD EAPCDDYHHC DFEEDLCDWD LRSLSKLKWI RTNQENISRT
DPWTGPGRDH SNNTASGYFL YVTVPDGGLT MDWAAFQSPR LQPTNSSHPC KMVMYTHQFG
PRSGGLTVLV ADQLIYPVWE RGGALGDLWV KAEVEIVSNY TFQILIMAAI RDLDYGGIAV
DSIVLSPECR WSSDNTTLEK FPKPPKNPCI DDPEKMCDFQ ADCDAAEDEA KCGDFSYPEG
SSGWTDTSIG SQGWLLDKSS TTGEFLYVAE AAGQQLTEAQ IRTPLLGPTG PVCNLSFDFA
LTGSLDHIGE LSVRVIDSLL GVRPNLWEFS GKTGAGDEEE TWQHVDVPIG VRKHRFQLAF
EARAVDVQPF AWIKVRNVQF ISCHANYIPS SPTGASCIFE DGLCAWYQDN SDNFDWSVVT
GMDHSIGVGT SLVVDMWSPS LRGAFGRLLS FPQQPTATES CLTFYYKLYG PNAGALNVKL
TDGLGYEILL WTRSGAHGNE WHEAHCPVPQ QNTNFQLMFE AVRSGFDGQV AIDDVAFLVG
PCTIPRKCSF EGQKCGYSSY GAINWLHRNG HTTTANGPKT DHTLGTELGY YMMVNTDADV
LPTGSAAVLI SPVQQGTTKP ECVSFWYHMT EGNPAFFTVY VKPQKGERVP IFSENLNEGD
DWRRVNGNVS VGLVSWQLEF EVVGSGSRGS HVAVDDITVS AHPCEDQGSK CSLENGMCSW
INIQDREREK LDWELTSPEK EKHYPVPPLD HTLGTEKGHF LFFPSSNRTA ANEKAWLVSP
QLPPIKPNCL RFWAYKPQSS DCQLRVWSLS GGIIYQQLIV NELSGPWRHF ELNITSREGY
QIVFEGIKGT SGFVALDDIE YTVGFDCATR DTKPTSKPDN AGGVAASVIV VVLLIGTLVA
LLVFYLRTEP DANSLSLAIG ISNEGYVPED PVTVPPRQNH PMAAGFNNVS PRSRTTPEES
LPL
//