ID T1FTX5_HELRO Unreviewed; 1835 AA.
AC T1FTX5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESO00769.1, ECO:0000313|EnsemblMetazoa:HelroP192410};
GN Name=20212272 {ECO:0000313|EnsemblMetazoa:HelroP192410};
GN ORFNames=HELRODRAFT_192410 {ECO:0000313|EMBL:ESO00769.1};
OS Helobdella robusta (Californian leech).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP192410, ECO:0000313|Proteomes:UP000015101};
RN [1] {ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ESO00769.1, ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:HelroP192410}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR EMBL; AMQM01005182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMQM01005183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMQM01005184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB096864; ESO00769.1; -; Genomic_DNA.
DR RefSeq; XP_009020940.1; XM_009022692.1.
DR STRING; 6412.T1FTX5; -.
DR EnsemblMetazoa; HelroT192410; HelroP192410; HelroG192410.
DR GeneID; 20212272; -.
DR KEGG; hro:HELRODRAFT_192410; -.
DR CTD; 20212272; -.
DR eggNOG; KOG1366; Eukaryota.
DR eggNOG; KOG2385; Eukaryota.
DR HOGENOM; CLU_237273_0_0_1; -.
DR InParanoid; T1FTX5; -.
DR OrthoDB; 2970602at2759; -.
DR Proteomes; UP000015101; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd02891; A2M_like; 1.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.60.40.1930; -; 1.
DR Gene3D; 2.60.40.690; Alpha-macroglobulin, receptor-binding domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR007941; DUF726.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR17920:SF3; TRANSMEMBRANE AND COILED-COIL DOMAIN-CONTAINING PROTEIN 4; 1.
DR PANTHER; PTHR17920; TRANSMEMBRANE AND COILED-COIL DOMAIN-CONTAINING PROTEIN 4 TMCO4; 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF05277; DUF726; 1.
DR Pfam; PF07678; TED_complement; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM01361; A2M_recep; 1.
DR SUPFAM; SSF49410; Alpha-macroglobulin receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000015101};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 767..905
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 1675..1765
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
FT REGION 16..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1008..1023
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1835 AA; 207368 MW; A57CBD2816003A9C CRC64;
MEKKFAKDED WIEVDDGMNH YSNSDSNNNN NNNKNSINNN NNNNKNNNNS NNNNDDLDYI
NDSSSSRKFN IDRNIVFDNS KTSEKIVVKN MNSNNNNSNK TDNNNNITNK NIKRANNNTQ
ANNNSNNSNT KLIGSKTQHD DITKQPKQGN NNNKNSNNNK SSSSNPITSF FTSLFADENS
NDNNCDDEDD ENNINNDNNN NNNNNHNGNN NNNNNNNNNN NNNNKTLVEN NYSSDKDFKE
NLVLIDKDTS ISNSKNNKNK KNNKNNNNNN NKDNNNNKNN SNPITSFFAS LFADETSVSN
NNNNNNNDGY DNDNNNKTNK NKNNNKKNNN KDDDVIHAIR DIDCHKDLAQ ENFALLDTDA
ISSNNNKNNN NKNNNNKKNN KKCEKNESDS RYDDNKNNNN DNNKDGDDDK NDVLSKCVLE
HFKDISPLSL FSYSHLVACT LCDLYGDSDE NRKFRNTFMW SFMERFGSEG KKFRPMMMLL
VNDEAVHEPG EMLLDEFKAT DLYLANGSKE VIRDLLMISI QRGEYDSRSR TFVKYMCQKL
DGLTAGLAAP LVAGSLGIAS GTIGTALFAT KAGVAIVGSL FGLAGAGLTG HKMNKRVGDL
DEFEFEELSG GKSLAVTIAV SGWLNDTYSD FRKVWLGLDE TPEQYTLNYE GKYLKELGGA
IHQFTQLGIS LAVNEGLKHT ILQGLLAAMM WPMALLSASS IIDNSWNVCT KRSNNAGIQL
AEVLLAREQG KRPVTLVGFG FGARVIFSCL KEMSTRQNYE GIVEQAILLG APVTSDGETW
RKVAKTESYM TFTLRVNFYT PEINYLISAG GNILLGSKLI MNSKQKTFSV ALSRKMAPSA
RIVAYCIVEG EVVMDSLTFF IKDSRLKQPE IILNYGKDFT RDTIEIVAKG PPGGYVFMNA
VDYEFSLRGA LPFITEQQVL HELMKYDSIA ASPYQFTWSM NDWYWEKTVF FPTQDTGMDT
NTTSFAAGLI VMSDANITIR QDFSPCNRSL GLGICPLSGQ CYELKTACDG VVHCSDGFDE
VACNPTPEEM YVPRPIELDS LFWNSRYQDT WLPFWKSTYI KQVGQGEIKI EQEELMDPLV
MGAFFMHPDQ GFSIAQEYIL HDTTRIFFVT IENPEKIRRG EQVGLRLDIY NYWDQDLEIL
ILLHGDDDYR FIVVEDFGYV VSYSPRTIRG DVQTMVSIKG NQVSTYQMFP IVATIPKGEI
TVRISTYSSQ RIDEEDVNIK ISYDGVVGRV RHTPYVVDLV NSGSLVIPDL KVNISERFVD
PGARDLYYIP YSNDATLYVY GDMVSPGFFD SHLTAMNTVH QYHDSGEVLA RQYAYMGSDG
EFRMFRRSGK PSVKLTAMAL KYLHAALTST WAEIIYVDVD ILNRIGNWLA SQQAPNGSFP
ETSDPYTVSK LTNETLMLHI PLTAHVVIAL SSAVRLTGNA RQKVDRAKTD GSNYLASQLA
VISDPFQMAI TSYALLVSNN RQADTAFNLL MNMRRRCLLI FCLIFLFQFQ YERQFHPNVG
NAVLATSYAL LGLLARNHKE DSVSTMKWVA SQHNRLMGWS STHDTIIALE AMTEFSYRQT
NRAFYNLQLD FRISPNATWF QRVKLDKTNF ANLFSFKLTP AYGQVLTRAS GTGYAMLAMD
TFIHFEKPYQ VEAVGPEFES FSLELDSQRF WGRNASHMEL NICFKWLRTD LAPAAGMTNV
IVDIPTGYVI SRDTIEWMYS AGFPGLKRVR FYEQQLITFF EYVSTTRTCF NFVADRWFPV
ANTSISHLLM IREYAETGMQ KLSAYNTYSL FQLHICQVCG SFQCPYCQYY NAATTRHRLT
FDHLGFNLVG TLIALYIVRF VSGQRYSIFG GGTGR
//
