ID G3SRK4_LOXAF Unreviewed; 1828 AA.
AC G3SRK4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=TSPO associated protein 1 {ECO:0000313|Ensembl:ENSLAFP00000002521.3};
GN Name=TSPOAP1 {ECO:0000313|Ensembl:ENSLAFP00000002521.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000002521.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000002521.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000002521.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000002521.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000002521.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the RIMBP family.
CC {ECO:0000256|ARBA:ARBA00010749}.
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DR STRING; 9785.ENSLAFP00000002521; -.
DR Ensembl; ENSLAFT00000003026.3; ENSLAFP00000002521.3; ENSLAFG00000003026.3.
DR eggNOG; KOG3632; Eukaryota.
DR GeneTree; ENSGT00950000183203; -.
DR HOGENOM; CLU_001979_1_0_1; -.
DR InParanoid; G3SRK4; -.
DR OMA; VSAPMPR; -.
DR TreeFam; TF316230; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0044305; C:calyx of Held; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0030156; F:benzodiazepine receptor binding; IEA:Ensembl.
DR GO; GO:0099626; F:voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels; IEA:Ensembl.
DR CDD; cd00063; FN3; 1.
DR CDD; cd12014; SH3_RIM-BP_1; 1.
DR CDD; cd12012; SH3_RIM-BP_2; 1.
DR CDD; cd12013; SH3_RIM-BP_3; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 3.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR035753; RIM-BP_SH3_2.
DR InterPro; IPR035755; RIM-BP_SH3_3.
DR InterPro; IPR040325; RIMBP1/2/3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14234:SF20; PERIPHERAL-TYPE BENZODIAZEPINE RECEPTOR-ASSOCIATED PROTEIN 1; 1.
DR PANTHER; PTHR14234; RIM BINDING PROTEIN-RELATED; 1.
DR Pfam; PF07653; SH3_2; 2.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00326; SH3; 3.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF50044; SH3-domain; 3.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50002; SH3; 3.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 647..714
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 878..969
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1592..1660
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1735..1802
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 26..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1316..1454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1467..1486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1513..1584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1793..1828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 123..193
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 224..251
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 411..515
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 41..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1104
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1377..1393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1521..1553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1814..1828
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1828 AA; 196303 MW; 48C51E022B4D6FB0 CRC64;
MEQLTSLPRP GDLGAMEPWA LPVWQSWIPG QGGEPGSTAP SVADTPATLQ VGKSRPGESS
EPEGAQSPGP VEGTESEGTL AGLPIPRQHA ESSGPSCPPK LEDEEVEASS KAKLNTGFGD
RPNLELLRAL GELQHRCAIL KEENQMLRKS SFPETEEKVR RLKRKNAELA VIAKRLEERA
RKLQETNLRV VSAPLPRPGA SLESCRKALA RQRARDLSET ASALLAKDKQ IAALQRECRE
LQARLTLAGK EGPPVASTCG NFDRASLREV PSGRVLPATE GRSPLRKPIS GGPTQPSRAQ
PAPSPPAGAV AREDANNPQV VVGDPEKPQR VQQLESELSK KRKKCQSLEQ EARKKQRRCE
ELELQLREAQ NENARLVEEN SQLSGRATEK EQVEWENAEL RGQLLGVTEE RDSALRKSQG
LQSKLESLEQ VLKHMREVAQ RRQQLEVEHE QARLSLQEKQ EEVRRLQQAQ AEAKREHEGA
VQLLESTLDS MQARVRELEE QCRSQTERFS LLAQELQAFR LHPGPLDLLT SALGCSAPGD
RLPPPCCCST CQPCRGSDSK DLDLPPGSPG HCTPKSSEPA SATLAGTPRR TAKKAESLSD
SSRSETIHNS PKSCPTPEVD TASEVEELEA DSVSLFPAAP EGTRGGSRIQ VFLARYSYNP
FEGPNENPEA ELPLTAGEYI YIYGNMDEDG FFEGELMDGR RGLVPSNFVE RVSDDDLLTT
LPPELADLSQ SSGPELSFLS GGGGGSSSGG QSSGGHSQPR PEEEDAGDEL SPSPSPDGLG
EPPAVPYPRR LVVLKQLAHS MVLAWEPPPE RVELHAYHIC VNGELRQALG PGAPLKAVLE
NLDLQAGLLH VSVRALTSQG SSDPLRCCLA VGARAGVGPS QLQVHRLTAT SAEITWVPSN
SNLHAIYLNG EECPPARPST YWATFCNLRP GTPYQARVEA QLPPRGSWEP GWERMEQRAA
TLQFTTLPAG PPDAPLDVQI EPGPSPGILI ISWLPVTIDV AGSSNGVRVT GYAIYADGQK
IMEVASPTAG SVLVELSQLQ LLRVCQEVAV RTMSTHGESA DSIPAPIAPA LALACLPAGV
PCPSPRPGSE ARPPLAPASP GPGDPSSPLR HSVPDGTQEP PGAPPASPSR EASKGSQEEP
PESCFQEEAG VAVLSTLEER RVSEPTVGER DPGPAAPELA QEEAEWRTGE AHPLSCSTQR
ALAQWAPCTE ASRGDTGSGL PARAEREDPA ELGARPVNSL VDHGRSSDLS DITLGSRPCS
FQKQVAGNSI RENGAKPPPL PDSSCETDSD EEILEQILEL PLQHFCSKKL FSIPGAGHFS
QDPSLSEPVL LGPGCDSSWP RGPGPCPLSP ELSRTGDCLE DVPGLVGGSS RRRGGGAPEK
PPSHRRPPDP REHCSRLLGN GGPQPSGRPG PTRERGSPPV SEGTRAGPEA GGRGRPPPSR
RCSRGRAPES GLASCLAPKC LEISIEYDSE DEQEADSGGI SITSSCYPGE GEAWRAASIG
RPRGPLKANL VSTPYLRLPA WEKGEPERRG RNATGRAKEP PSRATEMEEP RGQDSSGQRG
PPKRGARASR PVSSELAPPR SPPEEVLAYQ DLPVRIFVAL FDYDPVSMSP NPDAGEEELP
FREGQILKVF GDKDADGFYQ GEGGGRMGYI PCNMVAEVAV DSHSGRQQLL EQSYLSPDVL
VEGSEHSDAP HVFQVLEQLG LPPKPRRCQE KLAELEGPAQ PCTGPPKPVS SAGLKAPRLM
VAAFDYNPRE NSPNMDVEAE LPFQAGDVIT VFGSMDDDGF YYGELNGQRG LVPSNFLEGP
GPEARNLDRE PGTAPAESQR RRRRRVQC
//
