ID U3IWN4_ANAPP Unreviewed; 2049 AA.
AC U3IWN4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 2.
DT 24-JAN-2024, entry version 66.
DE SubName: Full=TSPO associated protein 1 {ECO:0000313|Ensembl:ENSAPLP00000011660.2};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000011660.2, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000011660.2, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000011660.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the RIMBP family.
CC {ECO:0000256|ARBA:ARBA00010749}.
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 STRING; 8840.ENSAPLP00000011660; -.
DR Ensembl; ENSAPLT00000012389.2; ENSAPLP00000011660.2; ENSAPLG00000011861.2.
DR GeneTree; ENSGT00950000183203; -.
DR HOGENOM; CLU_001979_1_0_1; -.
DR OMA; VSAPMPR; -.
DR Proteomes; UP000016666; Chromosome 20.
DR CDD; cd00063; FN3; 2.
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; 3.
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; 2.
DR SUPFAM; SSF50044; SH3-domain; 3.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50002; SH3; 3.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 588..655
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 719..812
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 815..906
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1748..1816
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1888..1955
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 498..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1279..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1345..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1573..1596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1686..1743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1836..1887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1966..2007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 26..96
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 127..180
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 272..327
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 352..449
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 500..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1466..1487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1706..1731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1858..1886
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1972..1991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2049 AA; 227534 MW; 261BC1D113A755CD CRC64;
MDGLGRERTD GLAQSGADYS FLVSQNTKLL SALEDLQHRY SSLMEENSLL RRSCFPETEE
KVKHLKRKNA ELAVIAKRLE ERARKLQEAN LKVVTAPVPL KGSSLELCKK AFACQRAKDL
TEQASALLAK DKQIEALQQE CRELQAKLIA GKDDPCCLNV VEFDRLLRES QKEVLRLQRQ
IALKNFKECL RSSKTSSGSS LPSATTCLGA TLNTCIKDSL LPKEARSGDP VLRVEAHRKV
EPGVLPLGIA SEGHENFPPR NAITDPESSQ QIQQLEFELK KKRKKCENLE HEVRKKHKRC
KELEIQLQEI QSENARLAEE NLQLNEKAGW AGQVESENAD LKLQVVLVTK ERDSVIQTNQ
GLQTKLENLE QVLKHMRDVA ERRQQLEAEH KEALLVLQEK QEEVRRLQQA QAEAKREHEG
AVQLLEARVK DLEEQCRNQT EQFSLLSQEL KQFRLQTGKI DLLTSTLVTS ELPLALCSSS
PQLHWEKDST GPALLTHQST KKVHNEETDE LESSQRVPDA AVGSPVSATG SQKQAKKVES
QSSSSKSESM QNSPKSCPTP EVDTASEMEE LDVDSISLMP ETGSQGPAKL QVFLARYSYN
PFDGPNENPE AELPLTAGEY IYIYGDMDED GFFEGELMDG RRGLVPSNFV ERISDDDLMT
FLPSELNDLT HSSYQEKSFV SASTSSGDKS DFSIEESSIS PLASRAEGDQ EEAVSHTAVP
YPRKLTLIKQ LARSIVVGWE PPLLPTGCPD IQSYNIYVDE ELRQNVKSGF QTKTVIEKLD
LKTKAYRVSV QSVTEQGSSD KLRCTFFVGQ DFCLAPTMLK VRSVTATSAE VTWLPCNSNY
NHAVYLNGEE CDITKPGVYW YAFRNLQPST QYVAKLEARP LKTPWEEVPE GQEQNSAVIH
FTTPLAGTPD APLDVQVEAG PSPGILVISW LPVTIDAEGS SNGVRVTGYA VYADGQKAIE
VTSPTAGSIL VDLSQLQMFQ VCREVSVRTM SLYGESVDSV PAQISSVLLR TSRHSSNSDS
AVSTTFTSRL PCRDPRGSLS ARSPPMHQTV ALLLQQVSTD ISDAKLTDLS SSHDGSARSL
PEKASSPLHL YSPSASLVHT IGTFPEGSGD AQDKKCLTVP PQQAGSTVFP GEGTEPGPSK
EAELKSSDKR TEVKMEQSVT KAPELETPSN SSLKIHMETC CTCSVEEPLK SPSTERERET
KEKHLTPEPV PAPGQADRTE GTSRDATAGG SSCQEFLRLS PGKEVMKEMS RVKREQEEKL
SEIGRRQLTL FAEHNRSSDL SDILEEEEED ELSSEALEEK KWDSREPFYR ENGEKMDLCD
TDSDEEILEK ILELPLQKNH SKKLFSIPEV TEDEDEDEDE KGVMEEKANV QDSLEMPTYH
AGRTEKPLSI QEPFLKADGS DSSPDLSAET PWDECTVKES RGDADHESPG FEPLGWSQKR
ANWNRGYQEN DPKPGTGAIP TQSKKKGNNY REKIWSQPEM GRKRQNDLSE HCSRLLGNCS
QMGSRLYRAP SLREELNIVS SAGGKEGFDV YNRARQGTSR RNHTNAVVSG FGEPALAAAL
CSSPRSLEID VEYDSEDDQD STCASPPESR LWPERSQSCA GDWSDCSSQS EVVHMDGRRD
LTRLEMLEEQ DMEWAGYPNH HLQFFCQEKE ALRCESSSEE QGWDLDCKSP VWRRRLEHPW
KGIRSTSLHK RASGNKDPRG QELSGSAAWQ APSRRGNRSV RRSQMQKPLL SSPGPPRSAA
SATAVKDDGI RIFVALFDYD PVSMSPNPDA AEEELPFKEG QILKVCGDKD ADGFYRGECA
GREGYIPCNM VSEIQVENNE IKRQLLKQGF LPADTPMESI GNGTFSPPPR RQTVPPPKPR
RSKKELDKQE KHKSQTGQKH QDFEAELLTP RSMMAVFDYN PKESSPNADA EAELTFSAGD
IITVFGSMDD DGFYYGELNQ QRGLVPSNFL EAVTSDGGMV EELHSKDKDA FPPSSESQLN
PDGSVDQSDS SPTPPTEPPS CLATGEQCPE QASLAILKCS DLPGQSKKKR GFFFKGKKLF
KKLGSSKKN
//
