ID H2NL39_PONAB Unreviewed; 1333 AA.
AC H2NL39;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=MIA SH3 domain ER export factor 2 {ECO:0000313|Ensembl:ENSPPYP00000006555.3};
GN Name=MIA2 {ECO:0000313|Ensembl:ENSPPYP00000006555.3};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000006555.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000006555.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000006555.3}
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 Ensembl; ENSPPYT00000006814.3; ENSPPYP00000006555.3; ENSPPYG00000005768.3.
DR eggNOG; ENOG502QUND; Eukaryota.
DR GeneTree; ENSGT00950000182767; -.
DR HOGENOM; CLU_258922_0_0_1; -.
DR InParanoid; H2NL39; -.
DR TreeFam; TF333137; -.
DR Proteomes; UP000001595; Chromosome 14.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR CDD; cd11892; SH3_MIA2; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR035555; MIA2_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23158:SF38; MELANOMA INHIBITORY ACTIVITY PROTEIN 2; 1.
DR PANTHER; PTHR23158; MELANOMA INHIBITORY ACTIVITY-RELATED; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Reference proteome {ECO:0000313|Proteomes:UP000001595};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1333
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035259058"
FT DOMAIN 39..101
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 260..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1074..1269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 646..799
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 869..1023
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 269..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1307
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1333 AA; 151395 MW; 7A52CAAF2E6328F2 CRC64;
MAKFGVHRIL LLAIYLTKCL ESTKLLADLK KCGDLECETL ISRVSAMRDY RGPDCRYLNF
TKGEEISVYV KLAGEREDLW AGSKGTEFGY FPRDAVQIEE VFISEEIQMS TKESDFLCLL
GVSYTFDNED SELNGDYGEN IYPYEEDKDE KSSIYESDFQ TEPGFYATYE STLFEDQVPA
LEAPEDIGST SESKDWEEVV VESMEQDHIP EVRVPPSSAV SGVKEWFGLG GEQAEEKAFE
SVIEPVQESS FRSRKIAVED ENDLEELNNG EPQTEHQQES ESEIDSVPKT QSELASESEH
IPKPQPTGWF GGGFTSYLGF GDEDTGLELI AEESNPPLQD FPNSISSDKE ATVPCTEILT
EKKDTITNDS LSLKPSWFDF GFAILGFAYA KEDKIMLDDR KNEEDGGADE HEHPLTSELD
PEKEQEIDMI KIIETEDRID KKPVLEKTDK SDTMPYLKKF LYNFDNPWNF QNIPKETELP
FPKQILDQNN VIENEETEEF SVDNYPTDNT KVMMFKSSYS LSEDASEFQI LKYLFQIDVY
DFMNSAFSPI VILTERVVAA LPEGMRPDSN PYGFPWELVI CAAVVGFFAV LFFSWRSFRS
VRREKKLAVM LSGLIEEKSK LLEKFSLVQK EYEGYEVESS LKNASFEKEA TEAQSLEATC
EKLNRSNSEL EDEILCLEKE LKEEKSKHSE QDELMADISK RIQSLEDESK SLKSQVAEAK
MTFKIFQMNE ERLKIAIKDA LNENSELQES QKQLLQDAEV WKEQVSELNK QKVTFEDSKV
HAEQVLNDKE NHIKTLTERL LKMKDWAAML GEDITDDDNL ELEMNSESEN GAYLDNPPKG
ALKKLIHAAK LNASLKTLEG ERNQIYIQLS EVDKTKEELT EHIKNLQTEQ ASLQSENTHF
ENENQKLQQK LKVMTELYQE NEMKLHRKLT VEENYRLEKE EKLSKVDEKI SHATEELETY
RKRAKDLEEE LERTIHSYQG QIISHEKKAH DNWLAARNAE RNLNDLRKEN AHNRQKLTET
ELKFELLEKD PYALDVPNTA FGREHSPYGP SPLGWPSSET RAFLSPPTLL EGPLRLSPLL
PGGGGRGSRG PGNPLDHQIT NERGESSCDR LTNPHRAPSD TGSLSPPWEQ DRRMMFPPPG
QSYPDSALPP QRQDRFCSNS GRLSGPAELR SFNMPSLDKM DGSMPSEMES SRNDTKDDLG
NLNVPDSSLP TENEATGPGF VPPPLAPIRG PLFPVDTRGP FLRRGPPFPP PPPGAVFGAS
RDYFPPRDFP GPPHAPFAMR NVYPPRGFPP YLPPRPGFFP PPPHSEGRSE FPSGLIPPSN
EPATEHPEPQ QET
//
