GenomeNet

Database: UniProt
Entry: A0A1S3ELZ5_DIPOR
LinkDB: A0A1S3ELZ5_DIPOR
Original site: A0A1S3ELZ5_DIPOR 
ID   A0A1S3ELZ5_DIPOR        Unreviewed;       672 AA.
AC   A0A1S3ELZ5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Signal recognition particle subunit SRP72 {ECO:0000256|ARBA:ARBA00018350, ECO:0000256|PIRNR:PIRNR038922};
GN   Name=Srp72 {ECO:0000313|RefSeq:XP_012864502.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012864502.1};
RN   [1] {ECO:0000313|RefSeq:XP_012864502.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012864502.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Component of the signal recognition particle (SRP) complex, a
CC       ribonucleoprotein complex that mediates the cotranslational targeting
CC       of secretory and membrane proteins to the endoplasmic reticulum (ER).
CC       {ECO:0000256|PIRNR:PIRNR038922}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|PIRNR:PIRNR038922}. Endoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004240}.
CC   -!- SIMILARITY: Belongs to the SRP72 family.
CC       {ECO:0000256|ARBA:ARBA00007676, ECO:0000256|PIRNR:PIRNR038922}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_012864502.1; XM_013009048.1.
DR   AlphaFoldDB; A0A1S3ELZ5; -.
DR   STRING; 10020.ENSDORP00000000156; -.
DR   GeneID; 105980287; -.
DR   KEGG; dord:105980287; -.
DR   CTD; 6731; -.
DR   InParanoid; A0A1S3ELZ5; -.
DR   OrthoDB; 91080at2759; -.
DR   Proteomes; UP000081671; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IEA:UniProtKB-UniRule.
DR   GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
DR   GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 4.
DR   InterPro; IPR013699; Signal_recog_part_SRP72_RNA-bd.
DR   InterPro; IPR026270; SRP72.
DR   InterPro; IPR031545; SRP72_TPR-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR14094; SIGNAL RECOGNITION PARTICLE 72; 1.
DR   PANTHER; PTHR14094:SF9; SIGNAL RECOGNITION PARTICLE SUBUNIT SRP72; 1.
DR   Pfam; PF08492; SRP72; 1.
DR   Pfam; PF17004; SRP_TPR_like; 1.
DR   Pfam; PF13181; TPR_8; 2.
DR   PIRSF; PIRSF038922; SRP72; 1.
DR   SMART; SM00028; TPR; 5.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS50005; TPR; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR038922};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW   ECO:0000256|PIRNR:PIRNR038922};
KW   Signal recognition particle {ECO:0000256|ARBA:ARBA00023135,
KW   ECO:0000256|PIRNR:PIRNR038922};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   REPEAT          227..260
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          533..589
FT                   /note="Signal recognition particle SRP72 subunit RNA-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF08492"
FT   REGION          528..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..586
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..645
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        658..672
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   672 AA;  74785 MW;  7CE3426D99A863D1 CRC64;
     MASSGSSGGA SVPALWSEVN RYGQNGDFTR ALKTVNKILQ INKDDITALH CKVICLIQNG
     SFKEALNVIN THTKVLTNNS LSFEKAYCEY RLNRIENALK TIENANQQSD KLKELYGQVL
     YRLERYDECL AVYRDLVRNS QDDYDEERKT NLSAVVAAQS NWEKVVPENL GLQEGTHELC
     YNAACALIGQ GQLNQAMKIL QKAEDLCRRS FSEDSDGTEE DPQAELAIIH GQMAYILQLQ
     GRTEEALQLY NQIIKLKPTD VGLLAVIANN IITINKDQNV FDSKKKVKLT NAEGVEFKLS
     KKQLQAIEFN KALLAMYTNQ AEQCRKISTS LQSQSPAHLL PVLIQAAQLC REKQHTKAIE
     LLQEFSDQHP ENAAEIKLTM AQLKISQGNI SKACLILRSI EELKHKPGMV SALVTMYSHE
     EDIDSAIEVF TQAIQWYQNH QPKSPAHLSL VREAANYKLK YGRKKEAISD LEQLWKQNPK
     DIHTLAQLIS AYSLVDPEKA KVLSKHLPSS DSMSLKIDVD ALENSPGATY IRKKGGKVTG
     DSQPKEQGQG DLKKKKKKKK GKLPKNYDPK VTPDPERWLP MRERSYYRGR KKGKKKDQIG
     KGTQGATAGA SSELDASKTV SSPPTSPRPG SAATVSASTS NIIPPRHQKP AGAPATKKKQ
     QQKKKKGGKG GW
//
DBGET integrated database retrieval system