Search Results
Overview
| Uniprot ID | F1RR78 |
|---|---|
| Protein Name | - |
| Gene Name | SPTAN1 |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1011 | QVEVLQKKFDDFQKD |
| 1189 | RADQRKAKLGDSHDL |
| 1274 | ASPEIKEKLDILEQE |
| 1446 | NIQSKHQKHQAFEAE |
| 1485 | AGSEEAVKARLAALA |
| 149 | LALQRQGKLFGAAEV |
| 1514 | QKLKEANKQQNFNTG |
| 1711 | VEHWKELKQLAAARG |
| 1818 | GKVSDLEKAAAQRKA |
| 1902 | KDQLLAAKHVQSKAI |
| 1907 | AAKHVQSKAIEARHA |
| 1933 | NSAARKKKLLEAQSH |
| 1982 | CNSLEEIKALREAHD |
| 209 | DLAALEDKVKALCAE |
| 211 | AALEDKVKALCAEAD |
| 2198 | RLNHQEFKSCLRSLG |
| 2270 | RALSSEGKPYVTKEE |
| 43 | KMREKGVKLLQAQKL |
| 512 | NLQGKVQKHQAFEAE |
| 561 | EVISLWKKLLEATEL |
| 702 | EETWIREKEPIAAST |
| 922 | VPAAYVKKLDPAQSA |
| 961 | SLLELGEKRKGMLEK |
| 968 | KRKGMLEKSCKKFML |
Function
Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane
Protein Sequence
10
MTWESHFHGC
20
NLWGGALNLQ
30
TRLTELHRQW
40
ELLLEKMREK
50
GVKLLQAQKL
60
VQFLRECEDV
70
MDWINDKEAI
80
VTSEELGQDL
90
EHVEVLQKKF
100
EEFQTDMAAH
110
EERVNEVNQF
120
AAKLVQEQHP
130
EEELIKTKQD
140
EVNAAWQRLK
150
GLALQRQGKL
160
FGAAEVQRFN
170
RDVDETISWI
180
KEKEQLMASD
190
DFGRDLASVQ
200
ALLRKHEGLE
210
RDLAALEDKV
220
KALCAEADRL
230
QQCHPLSATQ
240
IQVKREELIA
250
NWEQIRTLAA
260
ERHARLNDSY
270
RLQRFLADFR
280
DLTSWVTEMK
290
ALINADELAN
300
DVAGAEALLD
310
RHQEHKGEID
320
AHEDSFKSAD
330
ESGQALLAAG
340
HYASDEVREK
350
LAVLSEESAA
360
LLELWELRRQ
370
QYEQCMDLQL
380
FYRDTEQVDN
390
WMSKQEAFLL
400
NEDLGDSLDS
410
VEALLKKHED
420
FEKSLSAQEE
430
KITALDEFAT
440
KLIQNNHYAM
450
EDVATRRDAL
460
LSRRNALHER
470
AMYRRAQLAD
480
SFHLQQFFRD
490
SDELKSWVNE
500
KMKTATDEAY
510
KDPSNLQGKV
520
QKHQAFEAEL
530
SANQSRIDAL
540
EKAGQKLIDV
550
NHYAKDEVAA
560
RMNEVISLWK
570
KLLEATELKG
580
IKLREANQQQ
590
QFNRNVEDIE
600
LWLYEVEGHL
610
ASDDYGKDLT
620
NVQNLQKKHA
630
LLEADVAAHQ
640
DRIDGITIQA
650
RQFQDAGHFD
660
ADNIKKKQEA
670
LVARYEALKE
680
PMIARKQKLA
690
DSLRLQQLFR
700
DVEDEETWIR
710
EKEPIAASTN
720
RGKDLIGVQN
730
LLKKHQALQA
740
EIAGHEPRIK
750
AVTQKGNAMV
760
EEGHFAAEDV
770
KAKLSELNQK
780
WESLKSKASQ
790
RRQDLEDSLQ
800
AQQYFADANE
810
AESWMREKEP
820
IVGSTDYGKD
830
EDSAEALLKK
840
HEALMSDLSA
850
YGSSIQALRE
860
QAQSCRQQVA
870
PMDDETGKEL
880
VLALYDYQEK
890
SPREVTMKKG
900
DILTLLNSTN
910
KDWWKVEVND
920
RQGFVPAAYV
930
KKLDPAQSAS
940
RENLLEEQGS
950
IALRQEQIDS
960
QYHSLLELGE
970
KRKGMLEKSC
980
KKFMLFREAN
990
ELQQWINEKE
1000
AALTSEEVGA
1010
DLEQVEVLQK
1020
KFDDFQKDLK
1030
ANESRLKDIN
1040
KVAEDLESEG
1050
LMAEEVQAVQ
1060
QQEETDSKTA
1070
SPWKELNERW
1080
RSLQQLAEER
1090
SQLLGSAHEV
1100
QRFHRDADET
1110
KEWIEEKNQA
1120
LNTDNYGHDL
1130
ASVQALQRKH
1140
EGFERDLAAL
1150
GDKVNSLGET
1160
AERLIQSHPE
1170
AAEDLQEKCT
1180
ELNQAWSSLG
1190
KRADQRKAKL
1200
GDSHDLQRFL
1210
SDFRDLMSWI
1220
NGIRGLVSSD
1230
ELAKDVTGAE
1240
ALLERHQEHR
1250
TEIDARAGTF
1260
QAFEQFGQQL
1270
LAHGHYASPE
1280
IKEKLDILEQ
1290
ERTDLEKAWV
1300
QRRMMLDQCL
1310
ELQLFHRDCE
1320
QAENWMAARE
1330
AFLNTEDKGD
1340
SLDSVEALIK
1350
KHEDFDKAIN
1360
VQEEKIAALQ
1370
SFADQLIAAG
1380
HYAKGDISSR
1390
RNEVLDRWRR
1400
LKAQMIEKRS
1410
KLGESQTLQQ
1420
FSRDVDEIEA
1430
WISEKLQTAS
1440
DESYKDPTNI
1450
QSKHQKHQAF
1460
EAELHANADR
1470
IRGVIDTGNS
1480
LIERGACAGS
1490
EEAVKARLAA
1500
LADQWQFLVQ
1510
KSAEKSQKLK
1520
EANKQQNFNT
1530
GIKDFDFWLS
1540
EVEALLASED
1550
YGKDLASVNN
1560
LLKKHQLLEA
1570
DISAHEDRLK
1580
DLNSQADSLM
1590
TSSAFDTSQV
1600
KDKRDAINSR
1610
FQKIKGMAAS
1620
RRARLNESHR
1630
LHQFFRDMDD
1640
EESWIKEKKL
1650
LVSSEDYGRD
1660
LTGVQNLRKK
1670
HKRLEAELAA
1680
HEPAIQGVLD
1690
TGKKLSDDNT
1700
IGQEEIQQRL
1710
AQFVEHWKEL
1720
KQLAAARGQR
1730
LEESLEYQQF
1740
VANVEEEEAW
1750
INEKMTLVAS
1760
EDYGDTLAAI
1770
QGLLKKHEAF
1780
ETDFTVHKDR
1790
VKDVCANGQD
1800
LVKKNNHHEE
1810
NISSKMKGLN
1820
GKVSDLEKAA
1830
AQRKAKLDEN
1840
SAFLQFNWKA
1850
DVVESWIGEK
1860
ENSLKTDDYG
1870
RDLSSVQTLL
1880
TKQETFDAGL
1890
QAFQQEGIAN
1900
ITALKDQLLA
1910
AKHVQSKAIE
1920
ARHAALMKRW
1930
SQLLANSAAR
1940
KKKLLEAQSH
1950
FRKVEDLFLT
1960
FAKKASAFNS
1970
WFENAEEDLT
1980
DPVRCNSLEE
1990
IKALREAHDA
2000
FRSSLSSAQA
2010
DFNQLAELDR
2020
QIKSFRVASN
2030
PYTWFTMEAL
2040
EETWRNLQKI
2050
IKERELELQK
2060
EQRRQEENDK
2070
LRQEFAQHAN
2080
AFHQWIQETR
2090
SCMVEESGTL
2100
ESQLEATKRK
2110
HQEIRAMRSQ
2120
LKKIEDLGAA
2130
MEEALILDNK
2140
YTEHSTVGLA
2150
QQWDQLDQLG
2160
MRMQHNLEQQ
2170
IQARNTTGVT
2180
EEALKEFSMM
2190
FKHFDKDKSG
2200
RLNHQEFKSC
2210
LRSLGYDLPM
2220
VEEGEPDPEF
2230
EAILDTVDPN
2240
RDGHVSLQEY
2250
MAFMISRETE
2260
NVKSSEEIES
2270
AFRALSSEGK
2280
PYVTKEELYQ
2290
NLTREQADYC
2300
VSHMKPYVDG
2310
KGRELPTAFD
2320
YVEFTRSLFV
N
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0030864 | cortical actin cytoskeleton |
| Molecular Function | GO:0003779 | actin binding |
| Molecular Function | GO:0005509 | calcium ion binding |
| Molecular Function | GO:0005516 | calmodulin binding |
| Biological Process | GO:0051693 | actin filament capping |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.