ID F1S9I0_PIG Unreviewed; 1897 AA.
AC F1S9I0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 5.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=MIA SH3 domain ER export factor 3 {ECO:0000313|Ensembl:ENSSSCP00000011549.5};
GN Name=MIA3 {ECO:0000313|Ensembl:ENSSSCP00000011549.5,
GN ECO:0000313|VGNC:VGNC:108277};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000011549.5, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000011549.5, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000011549.5,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000011549.5}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004389}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
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DR PeptideAtlas; F1S9I0; -.
DR Ensembl; ENSSSCT00000011852.5; ENSSSCP00000011549.5; ENSSSCG00000010834.5.
DR VGNC; VGNC:108277; MIA3.
DR GeneTree; ENSGT00950000182767; -.
DR HOGENOM; CLU_002106_1_0_1; -.
DR TreeFam; TF333137; -.
DR Proteomes; UP000008227; Chromosome 10.
DR Bgee; ENSSSCG00000010834; Expressed in ovary and 45 other cell types or tissues.
DR ExpressionAtlas; F1S9I0; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR CDD; cd06503; ATP-synt_Fo_b; 1.
DR CDD; cd11893; SH3_MIA3; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23158; MELANOMA INHIBITORY ACTIVITY-RELATED; 1.
DR PANTHER; PTHR23158:SF54; TRANSPORT AND GOLGI ORGANIZATION PROTEIN 1 HOMOLOG; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1S9I0};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1897
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036473719"
FT DOMAIN 45..107
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 146..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1429..1454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1628..1751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1810..1897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1219..1295
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1338..1400
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1475..1523
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 153..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..183
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..743
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..881
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1645..1661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1846..1860
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1877..1897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1897 AA; 205824 MW; 3187664B13A0E98D CRC64;
MAAAPGLLLW LLLLGPPWPV PGQPEPAPGR RFSQDKVCAD EECSMLMYRG EALEDFTGPD
CRFVNFKKGD PVYVYYKLAG GSPEVWAGSV GRTFGYFPKD LIRVVHEYTQ EELQVPTDET
DFVCFDGGRD NFDNYNVEEL LGFLELYDSA PGDSEEVQEK TSQQVEEPPE ASEESDPEPE
PGEPSSQESE SVFSENTEEP RERQEAQKSH PHGSSQTDPA QGEQSSFEPF GEMLQDKLKV
PESERSKTSN SSQVSNEQEK IDAYKLLKTE MTLDLKTKFG STADAFVSDD ETTRFVTSLE
DDFDEELEGE YYTVGKEEEE NKDGVDDLPL LTFVDGEDPA PAKSGVEKHP TEKEQTWKEA
SRAGETQPPG IQYGEKNAEE DSTFSVVAEG EENTGADLET WDSKEAKAGD EASVPGRNVG
TARPASASGD PEEAADGLRK VEVPRSSQDQ DPEAPAELHV QGQGREAERP GRDLAAREAA
GLEDKTRRSG SRHASAQSGH PSPPPAAKED AETFLSAFAS KENDLEGAAV HISKDWPGKE
QPGAQRLEGG SEGASVARAA GIPGAERELG QAPSGIAAPR TDSQPDASRA RGEEDGGSGI
GPAPPPLSGE HLGEDQPGKS QNRTRFSSPD APAPPRNPGE EGPAPGSSLS GPQEGGAAAA
FPQQGSDDGG LSDQEAAEDA LEEGPAHRRE PAAAPREAGV TEVPGLRPEH PEADEDDYAP
EELLEDENAV SAKRSKEMSP EAEDAGLDAD PQASAKALLG AVHADPEPGE NKGETNNTVE
TGRKSDPAGE GVDARGGDPS SPVVEKGGSS LVGQKGQSPS EERDLPKRAN QTAGLGAASQ
HKAPDYFNED GLQEPPGAPG LLGKPGAELL KEDEEDVAKL VDAGLRGSAP EDQDSDPPPW
APHAPVQQEL GVPREDLPII GSFFKEQQSL ERFQKYFDVQ ELEALFQEMS SKLKSAQRES
LPYNVEKVLD KVFRASESHI LSVAEEMLDT RVTEDRDPAM RDSIFSEEAA VLDDVHELIY
FVRYTYSAKE EAASLAAAQP AEEGRPGPAE EGRPGPAEEG RPGPAEENIQ PPLEESGPQE
STAALTMQIP EEPSRVHQPV TRDMGPLEAS QKPETEKARN PGLFTTEGTP VMDAVGAKKQ
LETSAEEAAG VTPLDNAILL ICSMVFCLTK MLVATLPDDV QPGPDFYGLP WKPVLITAFL
GIVSFAIFFW RTILVVITEQ QISEKLKNIM KENAELVQKL SSYEQKIKES KKHVQETKKQ
NMILSDEAVK FKDKIKNLEE TNETLGDTAK SLRALLESER EQNAKNQDLI SENKKSIEKL
KDVISVNASE FSEVQIALNE AKLSEEKVKS ECHRVQEENA RLKKKKEQLQ EEIKDWSKAH
AELSEQIRSF ERAQQDLEVA LTHKDDNVNA LTNCITQLNC LDCESESEGQ NQGGNESDEL
ANGEAGGDRT EKMKSQIKQM MDRTLSVCKF LLPAVLSLTD QVKKLEEDCG SLQASKATLE
EECKTLRQKV EILNELYQQK EMALQKKLSQ EEFERQDREQ RLSAADEKVL LAAEEVKTYK
RRIEEMEDEL QKTERSFKNQ IATHEKKAHD NWLKARAAER AMAEERREAA NLRHRLLELT
QKMAMLQEEP VIVKPMPGRP NTQNPPRRGP LSQNGSFGPS PVSGGECSPP LTADPPARPL
SATLSRREMP RSDFGSVDGP PPRPRWPPEA SGKPSASGKG PECVQRVSGC GGGGQSILYS
SPKSVNMAAR GPPPFPGAPL LSSPGGGPLL PAIRYGPPPQ LCGPFGPRPL PPPFGPGLCP
PLGLREYAPG VPPGKRDLPL DPREFLPGHA PFRPVGPLGP REYFMPGARL PPPPHGPQDY
PPSSAARDLA PSGSRDEPQP ASPSAGQDCA QALKQSP
//
